THERAPEUTIC AND DIAGNOSTIC APPLICATIONS OF LAMININ AND LAMININ-DERIVED PROTEIN FRAGMENTS

Abstract: The invention relates to the discovery, identification and use of laminin, laminin-derived protein fragments, and laminin-derived polypeptides, as well as related peptides and antibodies, for the therapeutic intervention and diagnosis of Alzheimer's disease and other amyloidoses. In addition, the discovery and identification of an Alzheimer's beta-amyloid protein specific binding within the globular domain repeats of the laminin A chain, had led to new diagnostic and therapeutic applications for Alzheimer's disease and other amyloidoses which are disclosed.

Description: Title: THERAPEUTIC AND DIAGNOSTIC APPLICATIONS OF LAMININ AND LAMININ-DERIVED PROTEIN FRAGMENTS TECHNICAL FIELD The invention relates to the discovery, identification and use of laminin, laminin-derived protein fragments, and laminin-derived polypeptides, as well as related peptides and antibodies, for the therapeutic intervention and diagnosis of Alzheimer's disease and other amyloidoses. In addition, the discovery and identification of an Alzheimer's beta-amyloid protein (AJ3) specific binding region within the globular domain repeats of the laminin A chain, has led to new diagnostic and therapeutic applications for Alzheimer's disease and other amyloidoses which are disclosed. BACKGROUND OF THE INVENTION Alzheimer's disease is characterized by the accumulation of a 39-43 amino acid peptide termed the beta-amyloid protein or Aβ, in a fibrillar form, existing as extracellular amyloid plaques and as amyloid within the walls of cerebral blood vessels. Fibrillar AJ3 amyloid deposition in Alzheimer's disease is believed to be detrimental to the patient and eventually leads to toxicity and neuronal cell death, characteristic hallmarks of Alzheimer's disease. Accumulating evidence now implicates amyloid as a major causative factor of Alzheimer's disease pathogenesis. Discovery and identification of new compounds, agents, proteins, polypeptides or protein-derivatives as potential therapeutic agents to arrest Alzheimer's disease Aβ amyloid formation, deposition, accumulation and/or persistence is desperately sought. It is known that A13 is normally present in human blood and cerebrospinal fluid. However, it is not known why this potential fibrillar protein remains soluble in circulating biological fluids. Can the agent(s) responsible for this extraordinary solubility of fibrillar Aβ be applied to diagnostic and therapeutic regimens against the fibrillar AJ3 amyloid present in Alzheimer's brain? DISCLOSURE OF THE INVENTION Summary of the Invention The present invention provides answers to these questions and relates to the novel and surprising discovery that laminin and specific laminin-derived protein fragments are indeed potent inhibitors of Alzheimer's disease amyloidosis, and therefore have potential use for the therapeutic intervention and diagnosis of the amyloidoses. In addition, we have identified a specific region within laminin which interacts with the Alzheimer's disease beta-amyloid protein and contributes to the observed inhibitory and therapeutic effects. In addition, specific laminin-derived protein fragments which also interact with the Aβ of Alzheimer's disease have been discovered to be present in human serum and cerebrospinal fluid, and implicate diagnostic applications which are described. Laminin is a specific basement membrane component that is involved in several fundamental biological processes, and may play important roles in the pathogenesis of a number of different human diseases. Using a solid phase binding immunoassay, the present invention determined that laminin binds the Aβ of Alzheimer's disease with a single binding constant of K d = 2.7 X IO '9 M. In addition, using a Thioflavin T fluorometry assay (which quantitatively determines the amount of fibrillar amyloid formed), the present invention has determined that laminin is surprisingly an extremely potent inhibitor of Aβ fibril formation. In this latter study, 25 μM of A β (residues 1-40) was incubated at 37°C for 1 week in the presence or absence of 100 nM laminin. Laminin was found to significantly (pO.OOl) inhibit Aβ (1-40) amyloid fibril formation by 2.9-fold at 1 hour, 4.6-fold at 1 day, 30.6-fold at 3 days and 27.1-fold at 1 week. Other basement membrane components including perlecan, fibronectin and type IV collagen were not effective inhibitors of Aβ (1-40) fibrillogenesis in comparison to laminin, demonstrating the specificity of the inhibitory effect exhibited by laminin. The inhibitory effects of laminin on Aβ fibrillogenesis was also found to occur in a dose-dependent manner. In addition, laminin was found to cause dissolution of pre-formed Alzheimer's disease amyloid fibrils in a dose-dependent manner following 4 days of incubation. Laminin was digested with V8, trypsin or elastase to determine small protease-resistent fragments of laminin which still interacted with AJ3. A -55 kilodalton (kDa) laminin fragment derived from V8 or elastase digested laminin was found to interact with biotinylated Aβ (1-40). Amino acid sequencing of the -55 kDa fragment identified an Aβ-binding domain within laminin situated within the globular repeats of the laminin A chain. Intact laminin was found to be present in human serum but not human cerebrospinal fluid, whereas laminin protein fragments ranging from ~ 120 kDa to -200 kDa were found to be present in both human serum and cerebrospinal fluid. Of all the laminin protein fragments present in human biological fluids described above, a prominent -130 kilodalton band was found in human serum and cerebrospinal fluid which primarily interacted with Aβ as determined by ligand blotting methodology. This -130 kilodalton laminin fragment is known as the E8 fragment (i.e. generated following elastase digestion of laminin)(Yurchenco and Cheng, J. Biol. Chem. 268:17286-17299, 1993) and is also believed to consist of the globular domains of the laminin A chain. The interaction of specific laminin fragments such as the newly discovered -130 kDa protein is believed to bind A13 in biological fluids and keep it in a soluble state. The present invention describes the use of laminin, laminin-derived protein fragments, and laminin-derived polypeptides for the therapeutic intervention and diagnosis of Alzheimer's disease and other amyloidoses. In addition, the discovery and identification of a specific Alzheimer's Aβ-binding region within the globular domain repeats of the laminin A chain, and the discovery of the presence of laminin fragments containing this region in human serum and cerebrospinal fluid, has led to new diagnostic and therapeutic applications for Alzheimer's disease and other amyloidoses. Features of the Invention A primary object of the present invention is to establish new therapeutic methods and diagnostic applications for the amyloid diseases. The amyloid diseases include, but are not limited to, the amyloid associated with Alzheimer's disease and Down's syndrome (wherein the specific amyloid is referred to as beta-amyloid protein or Aβ), the amyloid associated with chronic inflammation, various forms of malignancy and Familial Mediterranean Fever (wherein the specific amyloid is referred to as AA amyloid or inflammation-associated amyloidosis), the amyloid associated with multiple myeloma and other B-cell dyscrasias (wherein the specific amyloid is referred to as AL amyloid), the amyloid associated with type II diabetes (wherein the specific amyloid is referred to as amylin or islet amyloid), the amyloid associated with the prion diseases including Creutzfeldt-Jakob disease, Gerstmann-Straussler syndrome, kuru and animal scrapie (wherein the specific amyloid is referred to as PrP amyloid), the amyloid associated with long-term hemodialysis and carpal tunnel syndrome (wherein the specific amyloid is referred to as beta 2 -microglobulin amyloid), the amyloid associated with senile cardiac amyloid and Familial Amyloidotic Polyneuropathy (wherein the specific amyloid is referred to as transthyretin or prealbumin), and the amyloid associated with endocrine tumors such as medullary carcinoma of the thyroid (wherein the specific amyloid is referred to as variants of procalcitonin). A primary object of the present invention is to use laminin, laminin-derived protein fragments and/or laminin-derived polypeptides as potent inhibitors of amyloid formation, deposition, accumulation and/or persistence in Alzheimer's disease and other amyloidoses. "Laminin fragments, laminin-derived fragments, laminin-derived protein fragments and/or laminin-derived polypeptides", may include, but are not limited to, laminin A (or Al) chain, laminin Bl chain, laminin B2 chain, laminin A2 chain (merosin), laminin Gl chain, the globular domain repeats within the laminin Al chain, SEQ ID NO: 1 (11 amino acid sequence within the mouse laminin A chain), SEQ ID NO: 2 (fourth globular repeat with the mouse laminin A chain), SEQ ID NO: 3 (fourth globular repeat within the human laminin A chain), SEQ ID NO: 4 (mouse laminin A chain), SEQ ID NO: 5 (human laminin A chain), SEQ ID NO: 6 (human laminin Bl chain), SEQ ID NO: 7 (mouse laminin Bl chain), SEQ ID NO: 8 (rat laminin B2 chain), SEQ ID NO: 9 (human laminin B2 chain), SEQ ID NO: 10 (mouse laminin Gl chain), SEQ ID NO: 11 (human laminin Gl chain), and all fragments or combinations thereof. Yet another object of the present invention is to use conformational dependent proteins, polypeptides, or fragments thereof for the treatment of Alzheimer's disease and other amyloidoses. Such conformational dependent proteins include, but are not limited to, laminin, laminin-derived fragments including laminin Al chain (SEQ ID NO 4; SEQ ID NO: 5), the globular repeat domains within the laminin Al chain (SEQ ID NO: 2, SEQ ID NO:3), an 11- amino acid peptide sequence within the globular domain of the laminin A chain (SEQ ID NO:l), laminin Bl chain (SEQ ID NO:6, SEQ ID NO: 7), laminin B2 chain (SEQ ID NO: 8, SEQ ID NO:9), laminin Gl chain (SEQ ID NO: 10, SEQ ID NO: 11) and/or portions thereof. Yet another aspect of the present invention is to use peptidomimetic compounds modelled from laminin, laminin-derived protein fragments and/or laminin-derived polypeptides, including but not limited to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10 and SEQ ID NO: 11, and fragments thereof, as potent inhibitors of amyloid formation, deposition, accumulation and/or persistence in Alzheimer's disease and other amyloidoses. Yet another object of the present invention is to mimic the 3-dimensional AB-binding site(s) on laminin, laminin-derived protein fragments and/or laminin-derived polypeptides and use these mimics as potent inhibitors of amyloid formation, deposition, accumulation and/or persistence in Alzheimer's disease and other amyloidoses. Yet a further aspect of the present invention is to use anti-idiotypic antibodies to laminin, laminin-derived protein fragments and/or laminin-derived polypeptides as potent inhibitors of amyloid formation, deposition, accumulation and/or persistence in Alzheimer's disease and other amyloidoses. Another aspect of the invention is to provide new and novel polyclonal and/or monoclonal peptide antibodies which can be utilized in a number of in vitro assays to specifically detect Aβ-binding laminin derived protein fragments and/or Aβ-binding laminin derived polypeptides in human tissues and/or biological fluids. Polyclonal or monoclonal antibodies that are made specifically against a peptide portion or fragment of laminin which interacts with Aβ can be utilized to detect and quantify amyloid disease specific laminin fragments in human tissues and/or biological fluids. These antibodies can be made by administering the peptides in antigenic form to a suitable host. Polyclonal or monoclonal antibodies may be prepared by standard techniques known to those skilled in the art. Another object of the present invention is to use laminin, the Aβ-binding laminin fragments and/or laminin-derived polypeptides referred to above, for the detection and specific localization of laminin peptides important in the amyloid diseases in human tissues, cells, and/or cell culture using standard immunohistochemical techniques. Yet another aspect of the present invention is to use antibodies recognizing laminin, any of the Aβ-binding laminin fragments, and/or laminin-derived polypeptides including, but not limited to, SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10 and SEQ ID NO: 1 1, and fragments thereof, for in vivo labelling; for example, with a radionucleotide, for radioimaging to be utilized for in vivo diagnosis, and/or for in vitro diagnosis. Yet another aspect of the present invention is to make use of laminin, Aβ-binding laminin protein fragments and or Aβ-binding laminin-derivedpolypeptides including, but not limited to, SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10 and SEQ ID NO: 11, and fragments thereof, as potential therapeutics to inhibit the deposition, formation, and accumulation of fibrillar amyloid in Alzheimer's disease and other amyloidoses (described above), and to enhance the clearance and/or removal of preformed amyloid deposits in brain (for Alzheimer's disease and Down's syndrome amyloidosis) and in systemic organs (for systemic amyloidoses) . Another object of the present invention is to use Aβ-binding laminin-derived polypeptides or fragments thereof, in conjunction with polyclonal and/or monoclonal antibodies generated against these peptide fragments, using in vitro assays to detect amyloid disease specific autoantibodies in human biological fluids. Specific assay systems can be utilized to not only detect the presence of autoantibodies against Aβ-binding laminin-derived protein fragments or polypeptides thereof in biological fluids, but also to monitor the progression of disease by following elevation or diminution of laminin protein fragments and/or laminin-derived polypeptide autoantibody levels. Another aspect of the invention is to utilize laminin, laminin-derived protein fragments and/or laminin-derived polypeptide antibodies and/or molecular biology probes for the detection of these laminin derivatives in human tissues in the amyloid diseases. Yet another object of the present invention is to use the laminin-derived protein fragments of the present invention in each of the various therapeutic and diagnostic applications described above. The laminin-derived protein fragments include, but are not limited to, the laminin Al chain, the globular repeats within the laminin Al chain, the laminin Bl chain, the laminin B2 chain, the laminin Gl chain, the laminin A2 chain (also known as merosin), and all constituents or variations thereof, including but not limited to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10 and SEQ ID NO: 11 , and fragments thereof, including peptides which have at least 70% homology to the sequences disclosed herein. Specific laminin-derived protein fragments or peptides as described above may be derived from any species including, but are not limited to, human, murine, bovine, porcine, and/or equine species. Another object of the invention is to provide polyclonal and/or monoclonal peptide antibodies which can be utilized in a number of in vitro assays to specifically detect laminin protein fragments in human tissues and/or biological fluids. Polyclonal or monoclonal antibodies made specifically against a peptide portion or fragment of any of the laminin fragments described herein can be utilized to detect and quantify laminin-derived protein fragments in human tissues and/or biological fluids. A preferred embodiment is a polyclonal antibody made to the - 130 kilodalton Aβ-binding laminin fragment present in human serum and cerebrospinal fluid. These antibodies can be made by isolating and administering the laminin-derived fragments and/or polypeptides in antigenic form to a suitable host. Polyclonal or monoclonal antibodies may be prepared by standard techniques by one skilled in the art. Yet another object of the present invention is to use laminin-derived fragment antibodies as described herein as a specific indicator for the presence and extent of laminin breakdown in brain by monitoring biological fluids including, but not limited to, cerebrospinal fluid, blood, serum, urine, saliva, sputum, and stool. Yet another object of the present invention is to use laminin-derived fragment antibodies as described herein as a specific indicator for the presence, extent and/or progression of Alzheimer's disease and/or other brain amyloidoses by monitoring biological fluids including, but not limited to, cerebrospinal fluid, blood, serum, urine, saliva, sputum, and stool. Yet another object of the present invention is to use laminin-derived fragment antibodies as described herein as a specific indicator for the presence and extent of laminin breakdown in systemic organs by monitoring biological fluids including, but not limited to, cerebrospinal fluid, blood, serum, urine, saliva, sputum, and stool. Yet another object of the present invention is to use laminin-derived fragment antibodies as described herein as a specific indicator for the presence and extent of amyloidosis in type II diabetes by monitoring biological fluids including, but not limited to, cerebrospinal fluid, blood, serum, urine, saliva, sputum, and stool. Yet another object of the present invention is to use laminin-derived fragment antibodies as described herein as a specific indicator for the presence and extent of amyloidosis in other systemic amyloidoses by monitoring biological fluids including, but not limited to, cerebrospinal fluid, blood, serum, urine, saliva, sputum, and stool. Yet another object of the present invention is to make use of peptides or fragments of laminin as described herein, including but not limited to, SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10 and SEQ ID NO: 11, and fragments thereof, as potential blocking therapeutics for the interaction of laminin and laminin-derived fragments in a number of biological processes and diseases (such as in Alzheimer's disease and other amyloid diseases described herein). Yet another object of the invention is to utilize specific laminin-derived fragment antibodies, as described herein, for the detection of these laminin fragments in human tissues in the amyloid diseases. Another object of the present invention is to use laminin, laminin-derived protein fragments, and laminin-derived polypeptides, as described herein, for the treatment of amyloid formation, deposition, accumulation and/or persistence in Alzheimer's disease and other amyloidoses. Another object of the present invention is to use pills, tablets, caplets, soft and hard gelatin capsules, lozenges, sachets, cachets, vegicaps, liquid drops, elixers, suspensions, emulsions, solutions, syrups, tea bags, aerosols (as a solid or in a liquid medium), suppositories, sterile injectable solutions,and sterile packaged powders, which contain laminin, laminin-derived protein fragments, and laminin-derived polypeptides, including, but not limited to, SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10 and SEQ ID NO: 1 1, and fragments thereof, to treat patients with Alzheimer's disease and other amyloidoses. Yet another object of the present invention is to use laminin, laminin-derived protein fragments, and laminin-derived polypeptides, including, but not limited to, SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10 and SEQ ID NO: 11, and fragments thereof, as potent agents which inhibit amyloid formation, amyloid deposition, amyloid accumulation, amyloid persistence, and/or cause a dissolution of pre-formed or pre-deposited amyloid fibrils in Alzheimer's disease, and other amyloidoses. Yet another object of the present invention is to provide the use of laminin, laminin-derived protein fragments, and laminin-derived polypeptides, as described herein, for inhibition of amyloid formation, deposition, accumulation, and/or persistence, regardless of its clinical setting. Yet another object of the present invention is to provide compositions and methods involving administering to a subject a therapeutic dose of laminin, laminin-derived protein fragments, and laminin-derived polypeptides, which inhibit amyloid deposition, including but not limited to, SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10 and SEQ ID NO: 11, and fragments thereof. Accordingly, the compositions and methods of the invention are useful for inhibiting amyloidosis in disorders in which amyloid deposition occurs. The proteins or polypeptides of the invention can be used therapeutically to treat amyloidosis or can be used prophylactically in a subject susceptible to amyloidosis. The methods of the invention are based, at least in part, in directly inhibiting amyloid fibril formation, and/or causing dissolution of preformed amyloid fibrils. Yet another object of the present invention is to provide pharmaceutical compositions for treating amyloidosis. The pharmaceutical compositions include a therapeutic compound of the invention in an amount effective to inhibit amyloid deposition and a pharmaceutically acceptable vehicle. These and other features and advantages of the present invention will become more fully apparent when the following detailed description of the invention is read in conjunction with the accompanying figures. BRIEF DESCRIPTION OF THE DRAWINGS The following drawings are illustrative of embodiments of the invention and are not meant to limit the scope of the invention. FIGURE 1 is a binding curve demonstrating the binding interaction of EHS laminin to substrate bound A13 (1-40). A single binding site with a K d = 2.7 X 10' 9 M is determined. FIGURE 2 demonstrates the potent inhibition of Aβ amyloid fibril formation by laminin as determined by a Thioflavin T fluorometry assay over a 1 week experimental period. FIGURE 3 compares the potent inhibition of Aβ amyloid fibril formation by laminin to other basement membrane components including fibronectin, type IV collagen and perlecan. Only laminin is found to have a potent inhibitory effect on Aβ fibrillogenesis as early as 1 hour after incubation. FIGURE 4 is a graph of a 1 week Thioflavin T fluorometry assay utilized to determine the potential dose-dependent effects of laminin on inhibition of Aβ amyloid fibril formation. Significant dose-dependent inhibition of Aβ (1-40) amyloid fibril formation is observed at 1 day, 3 days and 1 week of treatment with increasing concentrations of laminin. FIGURE 5 is a graph of a Thioflavin T fluorometry assay utilized to determine the potential dose-dependent effects of laminin on dissolution of pre-formed Aβ (1-40) amyloid fibrils within a 4 day incubation period. Laminin causes dissolution of pre-formed Aβ amyloid fibrils in a dose-dependent manner. FIGURE 6 is a graph of a 1 week Thioflavin T fluorometry assay utilized to determine the effects of laminin on islet amyloid polypeptide (amylin) fibrillogenesis, and determine whether laminin causes a dose-dependent inhibition of amylin fibril formation. Laminin does not significantly inhibit amylin fibrillogenesis suggesting its specificity for Alzheimer's disease amyloidosis. FIGURE 7 is a black and white photograph of laminin digested with V8 protease, separated by SDS-PAGE and following interaction with biotinylated Aβ (1-40). The smallest fragment of V8-resistent laminin that interacts with Aβ is a -55 kilodalton fragment. FIGURE 8 is a black and white photograph of laminin digested with trypsin, separated by SDS-PAGE and following interaction with biotinylated A13 (1-40). The smallest fragment of trypsin-resistent laminin that interacts with Aβ is a -30 kilodalton fragment. FIGURE 9 is a black and white photograph of laminin digested with elastase, separated by SDS-PAGE and following interaction with biotinylated AJ3 (1-40). A -55 kilodalton laminin fragment (arrow) that binds biotinylated Aβ was identified and sequenced. Note also the presence of a -130 kDa fragment (arrowheads) that binds Aβ following 1.5 hours of elastase digestion (lane 2). Panel A is a ligand blot using biotinylated Aβ as a probe, whereas panel B is Coomassie blue staining of the same blot in Panel A to locate the specific band(s) for sequencing. FIGURE 10 shows the complete amino acid sequence of the mouse laminin A chain. Sequencing of the -55 kilodalton Aβ-binding band shown in Figure 9 leads to the identification of an 11 amino acid segment (underline and arrowhead) within the laminin A chain. This A13 binding region of laminin is situated within the globular domain repeats of the laminin A Λ _chain. FIGURE 11 shows schematic diagrams of laminin and the newly discovered "A13 binding region" of laminin (shown in left panel; between the two arrowheads) which is situated within the last three globular domains of the laminin A chain. FIGURE 12 is a black and white photograph of a Western blot demonstrating the presence of laminin (arrowheads) and/or laminin-derived protein fragments (bands between the two arrows) in human serum (lanes 1-7; left side) and human cerebrospinal fluid (lanes 1-7; right side) obtained from Alzheimer's disease, type II diabetes and normal aged patients. A -110-130 kilodalton range of laminin positive protein fragments (between the two arrows) is present in both human serum and cerebrospinal fluid, whereas intact laminin (arrowheads) is only present in serum but not in cerebrospinal fluid. FIGURE 13 is a black and white photograph demonstrating that intact laminin (arrow) and a prominent -130 kilodalton band (arrowhead) present in human Alzheimer's disease, type II diabetes and normal aged patient serum, bind AJ3. The A β -binding laminin and specific AJ3-binding laminin fragments in human serum were identified following separation by SDS-PAGE and interaction with nanomolar concentrations of biotinylated Aβ (1-40). FIGURE 14 is a black and white photograph demonstrating the presence of a prominent -130 kilodalton band (arrow) in human Alzheimer's disease and normal aged patient cerebrospinal fluid, identified following separation by SDS-PAGE and following interaction with nanomolar concentrations of biotinylated A13 (1-40). This same -130 kilodalton Aβ-binding protein is also present in human serum (Figure 13). BEST MODE OF CARRYING OUT THE INVENTION The following sections are provided by way of additional background to better appreciate the invention. Alzheimer's Disease Alzheimer's disease is the most common cause of dementia in middle and late life, and is manifested by progressive impairment of memory, language, visuospatial perceptions and behavior (A Guide to the Understanding of Alzheimer's Disease and Related Disorders, edited by Jorm, New York University Press, New York 1987). A diagnosis of probable Alzheimer's disease can be made on clinical criteria (usually by the exclusion of other diseases, memory tests etc), but a definite diagnosis requires the histological examination of specific abnormalities in the brain tissue usually obtained at autopsy. In Alzheimer's disease, the parts of the brain essential for cognitive processes such as memory, attention, language, and reasoning degenerate, robbing victims of much that makes us human, including independence. In some inherited forms of Alzheimer's disease, onset is in middle age, but more commonly, symptoms appear from the mid-60's onward. Alzheimer's disease is characterized by the deposition and accumulation of a 39-43 amino acid peptide termed the beta-amyloid protein, A13 or β/A4 (Glenner and Wong. Biochem. Bionhvs. Res. Comm. 120:885-890, 1984; Masters et al, Proc. Natl. Acad. Sci. USA 82:4245-4249, 1985; Husby et al, Bull. WHO 71:105-108, 1993). Aβ is derived from larger precursor proteins termed beta-amyloid precursor proteins (or βPPs) of which there are several alternatively spliced variants. The most abundant forms of the β PPs include proteins consisting of 695, 751 and 770 amino acids (Tanzi et al, Nature 331:528-530, 1988; Kitaguchi et al, Nature 331:530-532, 1988; Ponte, et al, Nature 331:525-528, 1988). The small Aβ peptide is a major component which makes up the amyloid deposits of neuritic "plaques" and in the walls of blood vessels (known as cerebrovascular amyloid deposits) in the brains of patients with Alzheimer's disease. In addition, Alzheimer's disease is characterized by the presence of numerous neurofibrillary "tangles", consisting of paired helical filaments which abnormally accumulate in the neuronal cytoplasm (Grundke-Iqbal et al, Proc. Natl. Acad. Sci. USA 83:4913-4917, 1986; Kosik et al, Proc. Natl. Acad. Sci. USA 83:4044-4048. 1986; Lee et al, Science 251:675-678, 1991). The pathological hallmarks of Alzheimer's disease is therefore the presence of "plaques" and "tangles", with amyloid being deposited in the central core of plaques and within the blood vessel walls. It is important to note that a so-called "normal aged brain" has some amyloid plaques and neurofibrillary tangles present. However, in comparison, an Alzheimer's disease brain shows an over abundance of plaques and tangles. Therefore, differentiation of an Alzheimer's disease brain from a normal brain from a diagnostic point of view is primarily based on quantitative assessment of "plaques" and "tangles". In an Alzheimer's disease brain, there are usually thousands of neuritic plaques. The neuritic plaques are made up of extracellular deposits consisting of an amyloid core usually surrounded by enlarged axons and synaptic terminals, known as neurites, and abnormal dendritic processes, as well as variable numbers of infiltrating microglia and surrounding astrocytes. The neurofibrillary tangles present in the Alzheimer's disease brain mainly consist of tau protein, which is a microtubule-associated protein (Grundke-Iqbal et al, Proc. Natl. Acad. Sci. USA 83:4913-4917, 1986; Kosik et al, Proc. Natl. Acad. Sci. USA 83:4044-4048, 1986; Lee et al, Science 251:675-678, 1991). At the ultrastructural level, the tangle consists of paired helical filaments twisting like a ribbon, with a specific crossing over periodicity of 80 nanometers. In many instances within a neurofibrillary tangle, there are both paired helical filaments and straight filaments. In addition, the nerve cells will many times die, leaving the filaments behind. These tangles are known as "ghost tangles" since they are the filamentous remnants of the dead neuron. The other major type of lesion found in the brain of an Alzheimer's disease patient is the accumulation of amyloid in the walls of blood vessels, both within the brain parenchyma and in the walls of the larger meningeal vessels which lie outside the brain. The amyloid deposits localized to the walls of blood vessels are referred to as cerebrovascular amyloid or congophilic angiopathy (Mandybur, J. Neuropath. Exp. Neurol. 45:79-90, 1986; Pardridge et al, J. Neurochem. 49:1394-1401, 1987). In addition, Alzheimer's disease patients demonstrate neuronal loss and synaptic loss. Furthermore, these patients also exhibit loss of neuro transmitters such as acetylcholine. Tacrine, the first FDA approved drug for Alzheimer's disease is a cholinesterase inhibitor (Cutler and Sramek, New Engl. J. Med. 328:808-810, 1993). However, this drug has showed limited success, if any, in the cognitive improvement in Alzheimer's disease patients and initially had major side effects such as liver toxicity. For many years there has been an ongoing scientific debate as to the importance of "amyloid" in Alzheimer's disease and whether the "plaques" and "tangles" characteristic of this disease, were a cause or merely the consequences of the disease. Recent studies during the last few years have now implicated that amyloid is indeed a causative factor for Alzheimer's disease and not merely an innocent bystander. The Alzheimer's disease Aβ protein in cell culture has been shown to cause degeneration of nerve cells within short periods of time (Pike et al, Br. Res. 563:311-314, 1991: J. Neurochem. 64:253-265, 1994). Studies suggest that it is the fibrillar structure, a characteristic of all amyloids, that is responsible for the neurotoxic effects. The Aβ has also been found to be neurotoxic in slice cultures of hippocampus (the major memory region affected in Alzheimer's)(Harrigan et al, Neurobiol. Aging 16:779-789, 1995) and induces nerve cell death in transgenic mice (Games et al, Nature 373:523-527, 1995; Hsiao et al, Neuron 15:1203-1218, 1995). In addition, injection of the Alzheimer's Aβ into rat brain causes memory impairment and neuronal dysfunction (Flood et al, Proc. Natl. Acad. Sci. U.S.A. 88:3363-3366, 1991; Br. Res. 663:271-276, 1994), two additional hallmarks of Alzheimer's disease. Probably, the most convincing evidence that amyloid (ie. beta-amyloid protein) is directly involved in the pathogenesis of Alzheimer's disease comes from genetic studies. It has been discovered that the production of Aβ can result from mutations in the gene encoding, its precursor, known as the beta-amyloid precursor protein (Van Broeckhoven et al, Science 248:1120-1122, 1990; Europ. Neurol 35:8-19, 1995; Murrell et al. Science 254:97-99. 1991: Haass et al. Nature Med. 1:1291-1296, 1995). This precursor protein when normally processed usually only produces very little of the toxic AJ3. The identification of mutations in the amyloid precursor protein gene which causes familial, early onset Alzheimer's disease is the strongest argument that amyloid is central to the pathogenetic process underlying this disease. Four reported disease-causing mutations have now been discovered which demonstrate the importance of the beta-amyloid protein in causing familial Alzheimer's disease (reviewed in Hardy, Nature Genet. 1:233-234, 1992). All of these studies suggest that providing a drug to reduce, eliminate or prevent fibrillar Aβ formation, deposition, accumulation and/or persistence in the brains of human patients should be considered an effective therapeutic. Other Amyloid Diseases The "amyloid diseases" consist of a group of clinically and generally unrelated human diseases which all demonstrate a marked accumulation in tissues of an insoluble extracellular substance known as "amyloid", and usually in an amount sufficient to impair normal organ function. Rokitansky in 1842 (Rokitansky, "Handbuch der pathologischen Anatomie". Vol. 3, Braumuller and Seidel, Vienna) was the first to observe waxy and amorphous looking tissue deposits in a number of tissues from different patients. However, it wasn't until 1854 when Virchow (Virchow, Arch. Path. Anat. 8:416, 1854) termed these deposits as "amyloid" meaning "starch-like" since they gave a positive staining with the sulfuric acid-iodine reaction, which was used in the 1850's for demonstrating cellulose. Although cellulose is not a constituent of amyloid, nonetheless, the staining that Virchow observed was probably due to the present of proteoglycans (PGs) which appear to be associated with all types of amyloid deposits. The name amyloid has remained despite the fact that Friederich and Kekule in 1859 discovered the protein nature of amyloid (Friedrich and Kekule, Arch. Path. Anat. Physiol. 16:50, 1859). For many years, based on the fact that all amyloids have the same staining and structural properties, lead to the postulate that a single pathogenetic mechanism was involved in amyloid deposition, and that amyloid deposits were thought to be composed of a single set of constituents. Current research has clearly shown that amyloid is not a uniform deposit and that amyloids may consist of different proteins which are totally unrelated (Glenner, N. England J. Med. 302:1283-1292, 1980). Although the nature of the amyloid itself has been found to consist of completely different and unrelated proteins, all amyloids appear similar when viewed under the microscope due to amyloid's underlying protein able to adapt into a fibrillar structure. All amyloids regardless of the nature of the underlying protein 1) stain characteristically with the Congo red dye and display a classic red/green birefringence when viewed under polarized light (Puchtler et al, J. Histochem. Cytochem. 10:355-364, 1962), 2) ultrastructurally consists of fibrils with a diameter of 7-10 nanometers and of indefinite length, 3) adopt a predominant beta-pleated sheet secondary structure. Thus, amyloid fibrils viewed under an electron microscope (30,000 times magnification) from the post-mortem brain of an Alzheimer's disease patient would look nearly identical to the appearance of amyloid present in a biopsied kidney from a rheumatoid arthritic patient. Both these amyloids would demonstrate a similar fibril diameter of 7-10 nanometers. In the mid to late 1970's amyloid was clinically classified into 4 groups, primary amyloid, secondary amyloid, familial amyloid and isolated amyloid. Primary amyloid, is amyloid appearing de novo, without any preceding disorder. In 25-40% of these cases, primary amyloid was the antecedent of plasma cell dysfunction such as the development of multiple myeloma or other B-cell type malignancies. Here the amyloid appears before rather than after the overt malignancy. Secondary amyloid, appeared as a complication of a previously existing disorder. 10-15% of patients with multiple myeloma eventually develop amyloid (Hanada et al, J. Histochem. Cytochem. 19:1-15, 1971). Patients with rheumatoid arthritis, osteoarthritis, ankylosing spondylitis can develop secondary amyloidosis as with patients with tuberculosis, lung abscesses and osteomyelitis (Benson and Cohen, Arth. Rheum. 22:36-42, 1979; Kamei et al, Acta Path. Jpn. 32:123-133, 1982; McAdam et al, Lancet 2:572-575, 1975). Intravenous drug users who self- administer and who then develop chronic skin abscesses can also develop secondary amyloid (Novick, Mt. Sin. J. Med. 46:163-167, 1979). Secondary amyloid is also seen in patients with specific malignancies such as Hodgkin's disease and renal cell carcinoma (Husby et al, Cancer Res. 42:1600-1603, 1982). Although these were all initially classified as secondary amyloid, once the amyloid proteins were isolated and sequenced many of these turned out to contain different amyloid proteins. The familial forms of amyloid also showed no uniformity in terms of the peptide responsible for the amyloid fibril deposited. Several geographic populations have now been identified with genetically inherited forms of amyloid. One group is found in Israel and this disorder is called Familial Mediterranean Fever and is characterized by amyloid deposition, along with recurrent inflammation and high fever (Mataxas, Kidney 20:676-685, 1981). Another form of inherited amyloid is Familial Amyloidotic Polyneuropathy, and has been found in Swedish (Skinner and Cohen. Biochem. Biophvs. Res. Comm. 99:1326-1332, 1981), Portuguese (Saraiva et al, J. Lab. Clin. Med. 102:590-603, 1983; J. Clin. Invest. 74:104-119, 1984) and Japanese (Tawara et al. J. Lab. Clin. Med. 98:811-822, 1981) nationalities. Amyloid deposition in this disease occurs predominantly in the peripheral and autonomic nerves. Hereditary amyloid angiopathy of Icelandic origin is an autosomal dominant form of amyloid deposition primarily affecting the vessels in the brain, and has been identified in a group of families found in Western Iceland (Jennson et al, Clin. Genet. 36:368-377, 1989). These patients clinically have massive cerebral hemorrhages in early life which usually causes death before the age of 40. The primary, secondary and familial forms of amyloid described above tend to involve many organs of the body including heart, kidney, liver, spleen, gastrointestinal tract, skin, pancreas, and adrenal glands. These amyloid diseases are also referred to as "systemic amyloids" since so many organs within the body demonstrate amyloid accumulation. For most of these amyloidoses, there is no apparent cure or effective treatment and the consequences of amyloid deposition can be detrimental to the patient. For example, amyloid deposition in kidney may lead to renal failure, whereas amyloid deposition in heart may lead to heart failure. For these patients, amyloid accumulation in systemic organs leads to eventual death generally within 3 to 5 years. Isolated forms of amyloid, on the other hand, tend to involve a single organ system. Isolated amyloid deposits have been found in the lung, and heart (Wright et al, Lab. Invest. 30:767-773, 1974; Pitkanen et al, Am. J. Path. 117:391-399, 1984). Up to 90% of type II diabetic patients (non-insulin dependent form of diabetes) have isolated amyloid deposits in the pancreas restricted to the beta cells in the islets of Langerhans (Johnson et al, New Engl. J. Med. 321:513-518, 1989; Lab. Invest. 66:522-535, 1992). Isolated forms of amyloid have also been found in endocrine tumors which secrete polypeptide hormones such as in medullary carcinoma of the thyroid (Butler and Khan, Arch. Path. Lab. Med. 110:647-649, 1986; Berger et al, Virch. Arch. A Path. Anat. Hist. 412-543-551, 1988). A serious complication of long term hemodialysis is amyloid deposited in the medial nerve and clinically associated with carpal tunnel syndrome (Gejyo et al, Biochem. Biophys. Res. Comm. 129:701-706, 1985: Kidney Int. 30:385-390, 1986). By far, the most common type and clinically relevant type of organ-specific amyloid, and amyloid in general, is that found in the brains of patients with Alzheimer's disease (see U.S. Patent No. 4,666,829 and Glenner and Wong, Biochem. Biophys. Res. Comm. 120:885-890, 1984; Masters et al, Proc. Natl. Acad. Sci., USA 82:4245-4249, 1985). In this disorder, amyloid is predominantly restricted to the central nervous system. Similar deposition of amyloid in the brain occurs in Down's syndrome patients once they reach the age of 35 years (Rumble et al, New England J. Med. 320:1446-1452, 1989; Mann et al, Neurobiol. Aging 10:397-399, 1989). Other types of central nervous system amyloid deposition include rare but highly infectious disorders known as the prion diseases which include Creutzfeldt-Jakob disease, Gerstmann-Straussler syndrome, and kuru (Gajdusek et al, Science 197:943-960, 1977; Prusiner et al, Cell 38:127-134, 1984; Prusiner, Scientific American 251:50-59. 1984; Prusiner et al, Micr. Sc. 2:33-39, 1985; Tateishi et al, Ann. Neurol. 24:35-40, 1988). It was misleading to group the various amyloidotic disorders strictly on the basis of their clinical features, since when the major proteins involved were isolated and sequenced, they turned out to be different. For example, amyloid seen in rheumatoid arthritis and osteoarthritis, now known as AA amyloid, was the same amyloid protein identified in patients with the familial form of amyloid known as Familial Mediterranean Fever. Not to confuse the issue, it was decided that the best classification of amyloid should be according to the major protein found, once it was isolated, sequenced and identified. Thus, amyloid today is classified according to the specific amyloid protein deposited. The amyloid diseases include, but are not limited to, the amyloid associated with Alzheimer's disease, Down's syndrome and hereditary cerebral hemorrhage with amyloidosis of the Dutch type (wherein the specific amyloid is now known as the beta-amyloid protein or Aβ), the amyloid associated with chronic inflammation, various forms of malignancy and Familial Mediterranean Fever (AA amyloid or inflammation-associated amyloidosis), the amyloid associated with multiple myeloma and other B-cell abnormalities (AL amyloid), the amyloid associated with type II diabetes (amylin or islet amyloid), the amyloid associated with the prion diseases including Creutzfeldt-Jakob disease, Gerstmann-Straussler syndrome, kuru and animal scrapie (PrP amyloid), the amyloid associated with long-term hemodialysis and carpal tunnel syndrome (beta 2 -microglobulin amyloid), the amyloid associated with senile cardiac amyloid and Familial Amyloidotic Polyneuropathy (prealbumin or transthyretin amyloid), and the amyloid associated with endocrine tumors such as medullary carcinoma of the thyroid (variants of procalcitonin). Laminin and Its Structural Domains Laminin is a large and complex 850 kDa glycoprotem which normally resides on the basement membrane and is produced by a variety of cells including embryonic, epithelial and tumor cells (Foidart et al, Lab. Invest. 42:336-342, 1980; Timpl et al, Methods Enzvmol. 82:831-838, 1982). Lamιmn-1 (is derived from the Engelbreth-Holm-Swarm tumor) and is composed of three distinct polypeptide chains, A, Bl and B2 (also referred to as alpha 1, Bl and gamma- 1, respectively), joined in a multidomain structure possessing three shorts arms and one long arm (Burgeson et al, Matrix Biol. 14:209-211, 1994). Each of these arms is subdivided into globular and rodlike domains. Studies involving in vitro self-assembly and the analysis of cell-formed basement membranes have shown that laminin exists as a polymer, forming part of a basement membrane network (Yurchenco et al, J. Biol. Chem. 260:7636-7644, 1985: Yurchenco et al, J. Cell Biol. 117: 1119-1133, 1992; Yurchenco and Cheng, J. Biol. Chem. 268: 17286-17299, 1993). Laminm is believed to play important roles in a number of fundamental biological processes including promotion of neural crest migration (Newgreen and Thiery, Cell Tissue Res. 211:269-291, 1980; Rovasio et al, J. Cell Biol. 96:462-473, 1983), promotion of neurite outgrowth (Lander et al. Proc. Natl. Acad. Sci. 82:2183-2187, 1985; Bronner-Fraser and Lalher. Cell Biol. 106:1321-1329, 1988), the formation of basement membranes (Klemman et al, Biochem. 22:4969-4974, 1983), the adhesion of cells (Engvall et al, J. Cell Biol. 103: 2457-2465, 1986) and is inducible in adult brain astrocytes by injury (Liesi et al, EMBO J. 3:683-686, 1984). Laminin interacts with other components including type IV collagen (Terranova et al, Cell 22:719-726, 1980; Rao et al, Biochem. Biophvs. Res. Comm. 128:45-52, 1985; Charoms et al, J. Cell Biol. 100: 1848-1853, 1985; Laurie et al, J. Mol. Biol. 189:205-216, 1986), heparan sulfate proteoglycans (Riopelle and Dow, Brain Res. 525:92-100, 1990; Battagha et al, Eur. J. Biochem. 208:359-366, 1992) and heparin (Sakashita et al, FEBS Lett. 116:243-246, 1980; Del Rosso et al, Biochem. J. 199:699-704, 1981: Skubitz et al. J. Biol. Chem. 263:4861-4868, 1988). Several of the functions of laminin have been found to be associated with the short arms. First, the short arms have been found to participate in laminin polymerization (Yurchenco et al, J. Cell Biol. 117: 1119-1133, 1992; Yurchenco and Cheng, J. Biol. Chem. 268- 17286-17299, 1993) A recently proposed three-arm interaction hypothesis of laminin polymerization (Yurchenco and Cheng, J. Biol. Chem. 268: 17286-17299, 1993) further holds that self-assembly is mediated through the end regions of each of the three short arms A prediction of this model is that each short arm can independently and competitively inhibit laminin polymerization. However, it has not been possible to formally test this prediction using conventional biochemical techniques because of an inability to separate the alpha and gamma chains. Second, several heparin binding sites have been thought to reside in the short arms (Yurchenco et al. J BioI. Chem. 265.3981-3991, 1990: Skubitz et al. J. Cell Biol. 115:1137-1148, 1991), although the location of these sites have remained obscure Third, the alpha lfil integrin has been found to selectively interact with large short arm fragments containing all or most of the short arm domains (Hall et al, J. Cell B oL 110:2175-2184. 1990: Goodman et al. J Cell Biol 113:931-941, 1991). Most functional activities of laminin appear to be dependent upon the conformational state of the glycoprotein. Specifically, self-assembly and its calcium dependence, nidogen (entactin) binding to laminin, alphaββl integrin recognition of the long arm, heparin binding to the proximal G domain (cryptic) and RGD-dependent recognition of the short A chain of laminin (cryptic) have all been found to be conformationally dependent (Yurchenco et al, J Biol. Chem. 260:7636-7644, 1985; Fox et al, EMBO J. 10:3137-3146, 1991; Sung et al, J Cell Biol. 123:1255-1268, 1993). Two consequences of improperly folded laminin, loss of normal functional activity and the activation of previously cryptic activities, suggest that it is important to map and characterize biological activities using correctly folded laminin or conformational homologues to any particular laminin or laminin fragment. Laminin may also be involved in the pathogenesis of a number of important diseases. For example, in diabetes significant decrease in the levels of laminin on the glomerular basement membranes indicates that a molecular imbalance occurs (Shimomura and Spiro, Diabetes 36:374-381, 1987). In experimental AA amyloidosis (ie. inflammation-associated amyloidosis), increased levels of laminin are observed at the sites of AA amyloid deposition (Lyon et al, Lab. Invest. 64:785-790, 1991). However, the role(s) of laminin in systemic amyloidosis is not known. In Alzheimer's disease and Down's syndrome, laminin is believed to be present in the vicinity of Aβ-containing amyloid plaques (Perlmutter and Chui, Brain Res. Bull. 24:677-686, 1990; Murtomaki et al, J. Neurosc. Res. 32:261-273, 1992; Perlmutter et al, Micro. Res. Tech. 28:204-215, 1994). Previous studies have indicated that the various isoforms of the beta-amyloid precursor proteins of Alzheimer's disease, bind both the basement membrane proteins perlecan (Narindrasorasak et al, J. Biol. Chem. 266: 12878-12883, 1991) and laminin (Narindrasorasak et al, Lab. Invest. 67:643-652, 1992). With regards to laminin, it was not previously known whether laminin interacts with Aβ, whether a particular domain of laminin (if any) participates in Aβ interactions, and whether laminin had any significant role(s) in A13 amyloid fibrillogenesis. The present invention has discovered that laminin binds Aβ with relatively high affinity and surprisingly laminin is a potent inhibitor of Aβ amyloid formation, and causes dissolution of pre-formed Alzheimer's disease amyloid fibrils. In addition, a 55-kilodalton elastase resistent fragment of laminin which also binds AJ3 has been localized to the globular domain repeats within the A chain of laminin. This region is believed to be responsible for many of the inhibitory effects that laminin has on Alzheimer's disease amyloidosis. These findings indicate that laminin, laminin-derived protein fragments and/or laminin-derived polypeptides, particularly those containing the disclosed Aβ-binding site within the globular domain repeats within the laminin A chain, may serve as novel inhibitors of Aβ amyloidosis in Alzheimer's disease and other amyloidoses. In addition, the discovery and identification of an Alzheimer's Aβ-binding region within the globular domain repeats of the laminin A chain, and the discovery of its presence in human serum and cerebrospinal fluid, as a -130 kDa laminin-derived fragment, leads to novel diagnostic and therapeutic applications for Alzheimer's disease and other amyloidoses. Examples The following examples are provided to disclose in detail preferred embodiments of the binding interaction of laminin with Aβ, and the potent inhibitory effects of laminin and disclosed fragments on A13 fibril formation. However, it should not be construed that the invention is limited to these specific examples. Example 1 Binding of Laminin to the Beta-Amyloid Protein (Aβ) of Alzheimer's Disease 2 μg of Aβ (l-40)(Bachem Inc., Torrance, CA USA; Lot #WM365) in 40 μl of Tris-buffered saline (TBS)(pH 7.0) was allowed to bind overnight at 4°C to microtiter wells (Nunc plates, Maxisorb). The next day all of the microtiter wells were blocked by incubating with 300 μl of Tris-buffered saline containing 100 mM Tris-HCl, 50 mM NaCl, 0.05% Tween-20, and 3 mM NaN 3 (pH 7.4)(TTBS) plus 2% bovine serum albumin (BSA). Various dilutions (ie. 1:10, 1:30, 1:90, 1:270, 1:810, 1:2430 and 1:7290) of Engelbreth-Holm-Swarm (EHS) mouse tumor laminin (1 mg/ml)(Sigma Chemical Co., St. Louis, MO, USA) in 250 μl of TBS (pH 7.4) were placed in wells (in triplicate) either containing substrate bound AJ3 (1-40) or blank, and allowed to bind overnight at 4°C overnight. The next day, the wells were rinsed 3 times with TTBS, and then probed for 2 hours with 100 μl of rabbit anti-laminin antibody (Sigma Chemical Company, St. Louis, MO) diluted 1:10,000 in TTBS. After 3 rinses with TTBS, the wells were then incubated for 2 hours on a rotary shaker with 100 μl of secondary probe consisting of biotinylated goat anti-rabbit (1:1000) and strepavidin-peroxidase (1:500 dilution of a 2 μg/ml solution) in TTBS containing 0.1% BSA. The wells were then rinsed 3 times with TTBS and 100 μl of a substrate solution (OPD-Sigma Fast from Sigma Chemical Co., St. Louis, MO) was added to each well and allowed to develop for 10 minutes or until significant color differences were observed. The reaction was stopped with 50 μl of 4N H 2 S0 4 and read on a Model 450 microplate reader (Biorad, Hercules, CA USA) at 490 nm. Data points representing a mean of triplicate determinations were plotted and the affinity constants (ie. Kj) were determined using Ultrafit (version 2.1, Biosoft, Cambridge, U.K.) as described below. The binding data were analyzed assuming a thermodynamic equilibrium for the formation of the complex BL, from the laminin ligand in solution, L, and the uncomplexed Aβ adsorbed to the microtiter well, B, according to the equation: K d = [B] X [L]/[BL] We elected to determine K d 's by using an enzyme-linked immunoassay that gives a color signal that is proportional to the amount of unmodified laminin bound to Aβ (Engel, J. and Schalch, W., Mol. Immunol. 17:675-680, 1980; Mann, K. et al, Eur. J. Biochem. 178:71-80, 1988; Fox, J.W. et al, EMBO J. 10:3137-3146, 1991; Battaglia, C. et al, Eur. J. Biochem. 208:359-366, 1992). To account for potential non-specific binding, control wells without Aβ (in triplicate) were included for each concentration of laminin used in each binding experiment. Optical densities of the control wells never exceeded 0.050 at all laminin concentrations employed for these experiments. The optical densities of the control wells were subtracted from the optical densities of the AJ3-containing wells that received similar laminin concentrations. Non-specific absorbance obtained from Aβ containing wells that did not receive laminin were also subtracted from all data points. Thus, the equation in the form of: OD exp =OD 0 + (S x [laminin]) + (OD mflI x [laminin]/([laminin] + K where (S x [laminin]) represents non-specific binding (control wells) and OD 0 is the non-specific absorbance, becomes: OD exp = OD ma- x [laminin]/([laminin] + Kj) Therefore, at 50 % saturation, OD exp = 0.50 OD max and K d = [laminin]. Determination of [laminin] at 50% saturation was performed by non-linear least square program (Ultrafit from Biosoft, UK) using a one-site model. As demonstrated in Figure 1, EHS laminin bound immobilized Aβ (1-40) with a single binding constant with an apparent dissociation constant of K d = 2.7 X 10 '9 M. Several repeated experiments utilizing this solid phase binding immunoassay indicated that laminin bound Aβ (1-40) repetitively with one apparent binding constant. Example 2 Inhibition of Alzheimer's Disease Aβ Fibril Formation by Laminin The effects of laminin on A β fibrillogenesis was also determined using the previously described method of Thioflavin T fluorometry (Naiki et al, Lab. Invest. 65:104-110, 1991; Levine III, Protein Sci. 2:404-410, 1993; Levine III, Int. J. Exp. Clin. Invest. 2:1-6, 1995: Naiki and Nakakuki. Lab. Invest. 74:374-383, 1996). In this assay, Thioflavin T binds specifically to fibrillar amyloid and this binding produces a fluorescence enhancement at 480 nm that is directly proportional to the amount of amyloid fibrils formed (Naiki et al. Lab. Invest. 65:104-110, 1991; Levine III. Protein Sci. 2:404-410, 1993; Levine III. Int. J. Exp. Clin. Invest. 2:1-6, 1995; Naiki and Nakakuki, Lab. Invest. 74:374-383, 1996). In a first study, the effects of EHS laminin on Aβ (1-40) fibrillogenesis was assessed. For this study, 25 μM of freshly solubilized A§ (l-40)(Bachem Inc., Torrance, CA, USA; Lot # WM365) was incubated in microcentrifuge tubes at 37°C for 1 week (in triplicate), either alone, or in the presence of 100 nM EHS laminin (Sigma Chemical Company, St. Louis, MO, USA) in 100 mM Tris, 50 mM NaCl, pH 7.0 (TBS). 100 nM of laminin utilized for these studies represented a Aβdaminin molar ratio of 250:1. 50 μl aliquots were then taken from each tube for analysis at 1 hr, 1 day, 3 days, and 1 week. In a second set of studies, the effects of laminin on Aβ (1-40) fibril formation was directly compared to other basement membrane components including fibronectin, type IV collagen and perlecan. For these studies, 25 μM of freshly solubilized Aβ (1-40) was incubated in microcentrifuge tubes for 1 week (in triplicate) either alone, or in the presence of 100 nM of EHS perlecan (isolated as previously described)(Castillo et al, J. Biochem. 120:433-444, 1996), fibronectin (Sigma Chemical Company, St. Louis, MO, USA) or type IV collagen (Sigma Chemical Company, St. Louis, MO, USA). 50 ul aliquots were then taken for analysis at 1 hour, 1 day, 3 days and 1 week. In a third set of studies, 25μM of freshly solubilized Aβ (1-40) was incubated in microcentrifuge tubes for 1 week (in triplicate) either alone, or in the presence of increasing concentrations of laminin (i.e. 5 nM, 15 nM, 40 nM and 100 nM). 50 μl aliquots were taken for analysis at 1 hour, 1 day, 3 days and 1 week. For each determination described above, following each incubation period, Aβ peptides +/- laminin, perlecan, fibronectin or type IV collagen, were added to 1.2 ml of 100 μM Thioflavin T (Sigma Chemical Co., St. Louis, MO) in 50 mM phosphate buffer (pH 6.0). Fluorescence emission at 480 nm was measured on a Turner instrument-model 450 fluorometer at an excitation wavelength of 450 nm. For each determination, the fluorometer was calibrated by zeroing in the presence of the Thioflavin T reagent alone, and by seting the 50 ng/ml riboflavin (Sigma Chemical Co., St. Louis, Mo) in the Thioflavin T reagent to 1800 fluorescence units. All fluorescence determinations were based on these references and any background fluorescence given off by laminin, perlecan, type IV collagen, or fibronectin alone in the presence of the Thioflavin T reagent was always subtracted from all pertinent readings. As shown in Figure 2, freshly suspended Aβ (1-40) alone, following a 1 hour incubation at 37°C, demonstrated an initial fluorescence of 41 fluorescence umts. During the 1 week incubation period there was a gradual increase in the fluorescence of 25 μM AJ3 (1-40) alone, increasing 6.7-fold from 1 hour to 1 week, with a peak fluorescence of 379 fluorescence units observed at 1 week. This increase was significantly inhibited when Aβ (1-40) was co-incubated with laminin, in comparison to A13 alone. AJ3 (1-40) co-mcubated with laminin displayed fluorescence values that were 2.9-fold lower (p<0.001) at 1 hour, 4.6-fold lower (pO.OOOl) at 1 day, 30.6-fold lower (pO.OOOl) at 3 days and 27.1 -fold lower (pO.OOOl) at 1 week. This study indicated that laminin was a potent inhibitor of Aβ amyloid fibril formation, nearly completely inhibiting amyloid fibril formation even after 1 week of incubation. To determine whether the inhibitory effects of laminin was specific to this basement membrane component, an direct comparison was made to other known basement membrane components including perlecan, fibronectin, and type IV collagen. In these studies 25 μM of Aβ (1-40) was incubated in the absence or presence of either 100 nM of laminin, 100 nM of fibronectin, 100 nM of type IV collagen and 100 nM of perlecan (Figure 3). Freshly solubilized Aβ (1-40) when incubated at 37°C gradually increased in fluorescence levels from 1 hour to 1 week (by 10.8-fold)(Fιgure 3), as previously demonstrated (Figure 2). Perlecan was found to significantly accelerate Aβ (1-40) amyloid formation at 1 day and 3 days, whereas fibronectin and type IV collagen only showed significant inhibition of Aβ (1-40) fibrillogenesis at 1 week. Lammin, on the other hand, was again found to be a very potent inhibitor of A13 fibrillogenesis causing a 9-fold decrease at 1 and 3 days, and a 21-fold decrease at 1 week. This study reconfirmed the potent inhibitory effects of laminin on Aβ fibrillogenesis, and demonstrated the specificity of this inhibition, since none of the other basement membrane components (including fibronectin, type IV collagen and perlecan) were very effective inhibitors. To determine whether the inhibitory effects of laminin on AJ3 fibrillogenesis occurred in a dose-dependent manner, different concentrations of laminin (i.e. 5nM, 15 nM, 40 nM and 100 nM) were tested. As shown in Figure 4, freshly solubilized Aβ (1-40) when incubated at 37°C gradually increased from 1 hour to 1 week, as previously demonstrated (Figures 2 and 3). 100 nM of laminin significantly inhibited Aβ fibril formation at all time points studied, including 1 hour, 1 day, 3 days and 7 days. Laminin was also found to inhibit Aβ fibril formation in a dose-dependent manner which was significant (pθ.05) by 3 days of incubation. At 3 days and 7 days, both 100 nM and 40 nM of laminin significantly inhibited Aβ fibril formation. This study reconfirmed that laminin was a potent inhibitor of Aβ fibril formation and that this inhibition occurred in a dose-dependent manner. Example 3 Laminin Causes Dose-Dependent Dissolution of Pre-Formed Alzheimer's Disease Amyloid Fibrils The next study was implemented to determine whether laminin was capable of causing a dose-dependent dissolution of pre-formed Alzheimer's disease Aβ (1-40) amyloid fibrils. This type of activity would be important for any potential anti-Alzheimer's amyloid drug which can be used in patients who already have substantial amyloid deposition in brain. For example, Alzheimer's disease patients in mid-to late stage disease have abundant amyloid deposits in their brains as part of both neuritic plaques and cerebrovascular amyloid deposits. A therapeutic agent capable of causing dissolution of pre-existing amyloid would be advantageous for use in these patients who are at latter stages of the disease process. For this study, 1 mg of Aβ (l-40)(Bachem Inc., Torrance, CA, USA; Lot #WM365) was dissolved in 1.0 ml of double distilled water (lmg/ml solution) and then incubated at 37°C for 1 week. 25μM of fibrilhzed Aβ was then incubated at 37°C m the presence or absence of laminin (from EHS tumor; Sigma Chemical Company, St. Louis, MO, USA) at concentrations of 125 nM, 63 nM, 31 nM and 16 nM containing 150 mM Tris HCl, 10 mM NaCl, pH 7.0. Following a 4 day incubation, 50 μl aliquots were added to 1.2ml of lOOμM Thioflavin T (Sigma Chemical Co., St. Louis, MO) in 50mM NaPO 4 (pH 6.0) for fluorometry readings as described in example 2. As shown in Figure 5, dissolution of pre-formed Alzheimer's disease Aβ amyloid fibrils by laminin occurred in a dose-dependent manner. A significant (pO.OOl) 41% dissolution of pre-formed Aβ amyloid fibrils was observed with 125 nM of laminin, whereas 63 nM of laminin caused a significant (pO.OOl) 39% dissolution. Furthermore, 31 nM and 16 nM of laminin still caused a significant (pθ.01) 28% and 25% dissolution of pre-formed AJ3 amyloid fibrils These data demonstrated that laminm causes dissolution of pre-formed Alzheimer's disease amyloid fibrils in a dose -dependent manner following a 4-day incubation Example 4 Laminin Does Not Significantly Inhibit Islet Amyloid Polypeptide (Amylin) Fibril Formation In the next study, the specificity of the laminin inhibitory effects on Alzheimer's disease amyloid was determined by testing laminin's potential effects on another type of amyloid Amyloid accumulation occurs in the islets of Langerhans in -90% of patients with type II diabetes (Westermark et al, Am. J Path. 127:414-417, 1987). The major protein in islet amyloid is a 37 amino acid peptide, termed islet amyloid polypeptide or amylin which is known to be a normal secretory product of the beta-cells of the pancreas (Cooper et al, Proc Natl. Acad. Sci.. 84:8628-8632, 1987). The dose-dependent effects of laminin on amylin fibrillogenesis was determined using the Thioflavin T fluorometry assay. 25 μM of A§ (l-40)(Bachem Inc., Torrance, CA, USA; Lot #WM365) was incubated in microcentrifuge tubes at 37°C for 1 week (in triplicate), either alone, or in the presence of 5 nM, 15 nM, 40 nM and 100 nM of laminin in 150 mM Tris HCl, 10 mM NaCl, pH 7.0 (TBS). 50 μl aliquots were taken from each tube for analysis at 1 hr, 1 day, 3 days, and 1 week using Thioflavin T fluorometry as described in example 2. As shown in Figure 6, freshly suspended amylin alone following a 1-hour incubation at 37°C reached a maximum fluorescence of 1800 fluorescence units, which did not significantly change during the 1 week experimental period. The initial high fluorescence of amylin was attributed to amylin's ability to spontaneously form amyloid fibrils within a very short incubation period. Laminin at 100 nM did not significantly inhibit amylin fibril formation at all time points within the 1 week experimental period (Figure 6). In addition, no significant inhibition of amylin fibrillogenesis by laminin at decreasing concentrations (i.e. 40 nM , 15 nM and 5 nM) was observed, even though a decrease (but not significant) in amylin fibril formation was observed with 40 nM of laminin at 1 day, 3 days and 1 week (Figure 6). This study demonstrated that the inhibitory effects of laminin did not occur with amylin fibril formation, and demonstrated the specificity of the observed laminin inhibitory effects on Alzheimer's disease amyloid. Example 5 Identification of V8 and Trypsin-Resistent Laminin Fragments which Interact with the Beta-Amyloid Protein of Alzheimer's Disease In the next set of studies, we determined whether small fragment(s) of laminin generated by V8 or trypsin digestion would bind to Aβ. This would enable one to determine the domain(s) of laminin which bind Aβ and likely play a role in inhibition of AJ3 fibril formaφn and causing dissolution of preformed Alzheimer's amyloid fibrils (as demonstrated in the invention). For these experiments, AJ3 (1-40) was biotinylated according to the manufacturer's protocol (Pierce, Rockford, Illinois). For the ligand studies, intact EHS laminin was left undigested, or digested with V8 or trypsin (Sigma Chemical Company, St. Louis, MO, USA). More specifically, 2 μg of trypsin or V8 protease in 2 μl of 50 mM Tris-HCl buffer (pH 8.0) were added to 50 μl of laminin (50 μg)(in the same buffer) and incubated overnight at 37°C. The next day, 10 μl of protease-digested laminin (or undigested laminin) was mixed with 10 μl of 2X sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) sample buffer, and heated for 5 minutes in a boiling water bath. SDS-PAGE was performed according to the method of Laemmli (Laemmli, U.K. Nature 227:680-685, 1970), or according to the method of Schagger and Jagow (Schagger and Jagow, Anal. Biochem. 166:368-379, 1987) using a Mini-Protean II electrophoresis system (Biorad) with precast 4-15% Tris-Glycine or 10-20% tricine polyacrylamide gels, respectively, and under non-reducing conditions. Electrophoresis occurred at 200V for 45 minutes along with pre-stained molecular weight standards. After SDS-PAGE (10-20% tricine or 4-15% Tris-Glycine gels) was performed as described above, the separated laminin and its fragments (total protein of 10 μg/lane) were transferred to polyvinylidine difluoride membrane (PVDF) using a Mini transblot electrophoresis transfer cell (Biorad, Hercules, CA, U.S.A.). Electrotransfer was performed at 100V for 2 hours. Following transfer, membranes were rinsed with methanol and dried. The fragment(s) of laminin involved in binding to Aβ were then detected by using biotinylated- AJ3 (1-40), as described above. Blots were probed for 2 hours with 2 μM biotinylated Aβ (1-40) in TTBS. The membranes were then rinsed three times (10 seconds each) with TTBS, probed for 30 minutes with strepavidin alkaline phosphatase conjugate (Vectastain), rinsed again (as described above), and followed by the addition of an alkaline phosphatase substrate solution (Vectastain). Following color development, the reaction was stopped by flushing the membranes with double distilled water. As shown in Figure 7, V8-digested laminin produced multiple protein fragments which interacted with biotinylated Aβ (1-40). Using a 4-15% Tris-Glycine gel system (Figure 7, lane 1), V8-resistent laminin fragments which interacted with Aβ included fragments of -400 kDa (which probably represented intact laminin which was left undigested), -100-130 kDa, -85 kDa, and a prominent fragment at - 55 kDa. Using a 10-20% tricine gel system (Figure 7, lane 2), V8-resistent laminin fragments which interacted with Aβ included fragments of -130 kDa, -85 kDa, and a prominent fragment at - 55 kDa (Figure 7, lane 2, arrow). It is important to note that molecular size expressed in kilodaltons (kDa) are generally approximate. This study demonstrated that the smallest V8-resistent protein fragment of laminin which interacted with Aβ (1-40) was -55 kDa. As shown in Figure 8, trypsin-digested laminin produced multiple protein fragments which interacted with biotinylated Aβ (1-40). Using a 4-15% Tris-Glycine gel system (Figure 8, lane 1), trypsin-resistent laminin fragments which interacted with Aβ included fragments of -400 kDa (which probably represented intact laminin which was left undigested) , -150-200 kDa, -97 kDa, -65 kDa and a prominent fragment at - 30 kDa. Using a 10-20% tricine gel system (Figure 8, lane 2), trypsin-resistent laminin fragments which interacted with Aβ included fragments of -97 kDa, -90 kDa, -65 kDa and a prominent fragment at - 30 kDa (Figure 8, lane 2, arrow). This study demonstrated that the smallest trypsin-resistent fragment of laminin which interacted with Aβ (1-40) was -30 kDa. Example 6 Identification of Elastase-Resistent Laminin Fragments Which Interact with the Beta-Amyloid Protein of Alzheimer's Disease In the next set of studies, we determined whether small fragment(s) of laminin generated by elastase digestion would bind to Aβ. In addition , we sequenced and identified the region within elastase-resistent laminin which interacted with Aβ. For these experiments, Aβ (1-40) was biotinylated according to the manufacturer's protocol (Pierce, Rockford, Illinois). For the ligand studies, intact EHS laminin was left undigested, or digested with elastase (Sigma Chemical Company, St. Louis, MO, USA). For elastase digestion, 2 μg of elastase in 8 μl of 50 mM Tris-HCl buffer (pH 8.0) was added to 50 μl of laminin (50 μg)(in the same buffer) and incubated for 1.5 hours or 2.5 hours at 37°C. In addition, as a control, 2 μg of elastase in 50μl of 50 mM Tris-HCl buffer (pH 8.0) was incubated for 2.5 hours at 37°C. Following the appropriate incubation times as described above, 10 μl of each of the above incubations were mixed with 10 μl of 2X SDS-PAGE electrophoresis sample buffer, and heated for 5 minutes in a boiling water bath. SDS-PAGE was performed according to the method of Laemmli (Laemmli, Nature 227:680-685, 1970) using a Mini-Protean II electrophoresis system with precast 4-15% Tris-Glycine polyacrylamide gels, and under non-reducing conditions. Electrophoresis occurred at 200V for 45 minutes along with pre-stained molecular weight standards (Biorad). After SDS-PAGE was performed as described above, the separated laminin fragments were transferred to PVDF using a Mini transblot electrophoresis transfer cell (Millipore, Bedford, MA, U.S.A.). Electrotransfer was performed at 100V for 2 hours. Following transfer, membranes were rinsed with methanol, dried and cut into two equal parts which were used for Afi ligand blotting, or Coomassie blue staining and subsequent amino acid sequencing. The fragment(s) of laminin involved in binding to Aβ were then detected by using biotinylated-A13 (1-40), as described above. Blots were probed for 2 hours with 2 μM biotinylated A β (1-40) in TTBS. The membranes were then rinsed three times (10 seconds each) with TTBS, probed for 30 minutes with strepavidin alkaline phosphatase conjugate (Vectastain), rinsed again (as described above), and followed by the addition of an alkaline phosphatase substrate solution (Vectastain). Following color development, the reaction was stopped by flushing the membranes with double distilled water. For Coomassie blue staining, PVDF membranes were immersed with 0.2% Coomassie Brilliant blue (w/v) in 50 % methanol, 10% acetic acid, and 40% distilled water for 2 minutes, and then rinsed with 50% methanol, 10% acetic acid, and 40% distilled water until visible bands were observed, and no background staining was present. The 55 kDa Aβ-binding laminin fragment, described below, was sent to the Biotechnology Service Center (Peptide Sequence Analysis Facility at the University of Toronto, Toronto, Ontario, Canada) and subjected to amino acid sequencing using a Porton 2090 Gas-Phase Microsequencer (Porton Instruments, Tarzana, CA) with on-line analysis of phenylthiohydantoin derivatives. In Figure 9, Panel A represents an Aβ ligand blot whereas Panel B represents the equivalent Coomassie blue stained blot. As shown in Figure 9 (Panel A, lanes 2 and 3), elastase-digested laminin produced multiple protein fragments which bound biotinylated A13 (1-40). Panel A, lane 1 represents undigested mouse EHS laminin, whereas lanes 2 and 3 represents laminin which had been digested with elastase for 1.5 hours or 2.5 hours, respectively. Panel A, lane 4 represents elastase digestion for 2.5 hours in the absence of laminin. Undigested laminin (Fig. 9, Panel A, lane 1) which interacted with Λβ included multiple bands from > -400 kDa to >~86 kDa, with the most prominent Aβ-interaction occurring with intact laminin (i.e. - 400 kDa). Elastase-resistent laminin protein fragments which interacted with A β (Fig. 9, Panel A, lanes 2 and 3) included fragments of >~400kDa, - 130 kDa (arrowhead), -80-90 kDa, -65 kDa and a prominent band at - 55 kDa (arrow). The interaction of these elastase-resistent laminin protein fragments with Aβ were only observed under non-reducing conditions suggesting that the AJ3 interaction was also conformation dependent. The 130kDa elastase resistent laminin fragment which interacts with A13, is also believed to be part of the E8 fragment (see Figure 11), and is the same protein fragment of laminin that appears to be present in human serum and cerebrospinal fluid (see Examples 10 and 11). Figure 9, Panel A, lane 4 demonstrates that the band observed at -29 kDa represents non-specific Aβ binding due to the presence of the elastase enzyme alone. Figure 9, Panel B demonstrates all of the multiple protein bands which were stained by Coomassie blue. Note, for example, in Panel B, lanes 2 and 3, that elastase digestion of laminin produced multiple protein fragments between -55 kDa and -90 kDa which did not bind AJ3, and were not observed in the Aβ ligand blot (Fig. 9, Panel A, lanes 2 and 3). Example 7 An Aβ-Binding Domain Within Laminin is Identified Within the Globular Repeats of the Laminin A Chain The 55 kDa laminin fragment (ie. produced following 1.5 hours of elastase digestion) that demonstrated positive AJ3 binding interaction by ligand blotting was then prepared (Fig. 9, Panel B, lane 2, arrow) in large amounts for amino acid sequencing (as described in example 6). Sequence data determined the exact location within laminin that was involved in binding to Aβ. An 1 1 -amino acid sequence was determined from sequencing of the 55 kDa band. The sequence identified was: Leu-His-Arg-Glu-His-Gly-Glu-Leu-Pro-Pro-Glu (SEQ ID NO:l) The specific AB-binding domain within laminin was then identified by comparison to known mouse laminin sequence (Sasaki and Yamada, J. Biol. Chem. 262:17111-17117, 1987: Sasaki et al. Proc. Natl. Acad. Sci. 84:935-939, 1987; Durkin, et al, Biochem. 27:5198-5204, 1988; Sasaki et al, J. Biol. Chem. 263:16536-16544, 1988), since mouse EHS laminin was utilized in the studies of the present invention. In addition, the complete amino acid sequence within laminin was retrieved from the National Center for Biotechnology Information, Bethesda, Maryland, U.S.A. Figure 10 shows the complete amino acid sequence of mouse laminin A chain (Genebank accession number P19137; SEQ ID NO: 4). The 11 amino acid protein fragment sequenced from the -55 kDa protein within laminin which binds Aβ is identified (Figure 10; bold underline and arrowhead; SEQ ID NO: 1) and matches exactly to the region within the third globular domain repeat of laminin A chain (Figure 11). The fourth globular domain repeat of mouse laminin A chain is shown as SEQ ID NO: 2 (Genebank Accession Number P19137; amino acids #2746-2922), whereas the fourth globular domain repeat of human laminin A chain is shown as SEQ ID NO: 3 (Genebank Accession Number P25391; amino acids #2737-2913). Figure 11 shows two schematic representations of laminin (Colognato-Pyke et al, J. Biol. Chem. 270:9398-9406, 1995) and the newly discovered Aβ-binding region of laminin (shown in left panel; between the two arrowheads) which is situated within the last three globular domains of the laminin A chain. The left panel of figure 11 illustrates laminin and fragments generated following protease digestions. Elastase fragments El', E1X (dark line border), E-alpha-35 and E4 all correspond to regions of the short arms of laminin. Long arm fragments are E8, E3 and cathepsin G fragment C8-9. The E8 fragment produced by elastase digestion of laminin contains the long arm fragments containing the distal part of the long arm and the G subdomains 1-3, and consists of a 130-150 kda (Yurchenco and Cheng, J. Biol. Chem. 268:17286-17299, 1993).The E3 fragments also produced by elastase digestion of laminin contains the distal long arm globule with G subdomains 4 and 5. The E3 fragment shown in Figure 11, Panel A, has previously shown to be a doublet at -60 kDa and -55 kDa (Yurchenco and Cheng. J. Biol. Che . 268: 17286-17299. 1993). This also confirms our discovery whereby the -55 kDa fragment which we found to bind Aβ is localized within the E3 region of laminin (Figure 11, Left Panel). The right panel of Figure 11 depicts the function map with the alpha (A chain), β (Bl chain) and gamma (B2 chain) chains of laminin shown in shades of decreasing darkness. EGF repeats are indicated by bars in the rod domains of the short arm. Domains, based on sequence analysis, are indicated in small Roman numerals and letters. The locations of heparin-binding, polymer-forming, and the active alphalβl in te grin-binding sites are shown in bold-face for the alpha-chain short arm. The long arm functions of heparin binding (heparin), alphaδβl integrin-recognition site (alphaββl), and dystroglycan (DG), mapped in other studies, are indicated in gray-shaded labels. It is interesting to note that the Aβ-binding region of laminin is also a region involved in binding to heparin: It should also be emphasized that the globular domain repeats of the laminin A chain likely interacts with AJ3 in a conformation dependent manner, since the interaction of the ~55-kilodalton elastase-resistent protein fragments with Aβ was only observed under non-reducing conditions. Example 8 Identification of Laminin and Laminin Protein Fragments in Human Serum and Cerebrospinal Fluid Derived from Alzheimer's disease, Type II Diabetes, and/or Normal Aged Patients In the next study, western blotting techniques using a polyclonal antibody against laminin was used to determine whether intact laminin and/or laminin fragments were present in human serum and cerebrospinal fluid obtained from Alzheimer's disease, type II diabetes and/or normal aged patients. In this study, human serum was obtained from the Alzheimer's disease Research Center at the University of Washington from either living aged patients who may have had corresponding mini-mental state examinations (where a score of 30 is normal, a score of 15 suggests moderate dementia and a score <10 suggests severe dementia), or from living aged patients who had subsequently died and were diagnosed at autopsy with Alzheimer's disease (following examination of their brains obtained postmortem). In addition, human serum was obtained from the Diabetes Endocrinology Research Center at the University of Washington. The following human serums were obtained and analyzed as part of this study: 1) patient #9; a normal 67 yr old female with a mini-mental score of 30; 2) patient #5226 - a 70 year old female with confirmed moderate Alzheimer's disease who also had a mini-mental score of 12 ; 3) patient #5211- a 66 year old male with confirmed Alzheimer's disease who also had a mini-mental score of 25; 4) patient B- a 63 year old male who had confirmed type II diabetes; 5) patient #5223- a 68 year old female with confirmed Alzheimer's disease who also had a mini-mental score of 22; 6) patient #22- an 83 yr old normal aged female who also had a mini-mental score of 30; 7) patient #C- a 68 year old male with confirmed type II diabetes. Each of these serums were utilized in this study and represent lanes 1-7 (left side) of Figure 12 (in the same order as above). In addition, cerebrospinal fluid was obtained from the Alzheimer's disease Research Center at the University of Washington from either living aged patients who may have had corresponding mini-mental state examinations, or from living aged patients who had subsequently died and were diagnosed at autopsy with Alzheimer's disease (following examination of their brains obtained postmortem). The following human cerebrospinal fluids were obtained as part of this study: 1) patient #6- a normal 64 year old female who had a mini-mental score of 30; 2) patient #7- a normal 67 year old male who had a mini-mental score of 30; 3) patient #8- a normal 80 year old female who had a mini-mental score of 30; 4) patient #9- a normal 67 year old female who had a mini-mental score of 30; 5) patient #111 IP- a normal 78 year old female who had a mini-mental score of 30; 6) patient #50-a 66 year old male patient with probable moderate Alzheimer's disease as indicated by a mini-mental score of 15; 7) patient #54-a 73 year old male with probable severe Alzheimer's disease as indicated by a mini-mental score of 8. Each of these cerebrospinal fluid samples were utilized in this study and represent lanes 1-7 (right side) of Figure 12 (in the same order as above). For the study described above, 10 μl of human serum diluted at 1:10, or lOμl of undiluted human cerebrospinal fluid was added to 10 μl of SDS-PAGE buffer and ligand blots were prepared as in Example 6. Blots were probed for 2 hours with a polyclonal antibody (used at a dilution of 1:10,000 in TTBS) against EHS laminin (Sigma Chemical Company, St. Louis, MO). The membranes were then rinsed 3 times (10 seconds each) with TTBS and incubated for 1 hour with a biotinylated goat anti-rabbit IgG secondary antibody diluted 1: 1,000 with TTBS. The membranes were then rinsed three times (10 seconds each) with TTBS, probed for 30 minutes with strepavidin alkaline phosphatase conjugate (Vectastain), rinsed again (as described above), followed by the addition of an alkaline phosphatase substrate solution (Vectastain). Following color development, the reaction was stopped by flushing the membranes with double distilled water. As shown in Figure 12, intact laminin (arrowheads) was present in human serum (lanes 1-7; left side) but not in human cerebrospinal fluid (lanes 1-7; right side). Qualitative observations suggest that intact laminin (as described above) may have been decreased in serum of Alzheimer's disease patients in comparison to controls (i.e. compare intact laminin in Figure 12, lane 1, left side-normal individual; to Figure 12, lane 2, left side-Alzheimer's disease patient). In addition to intact laminin, human serum derived from Alzheimer's disease, type II diabetes and normal aged patients also contained laminin immunoreactivity in a series of band from -120 kDa to -200 kDa (Figure 12, bands observed between the tv/o arrows). On the other hand, cerebrospinal fluid samples did not contain intact laminin (Figure 12; lanes 1-7; right side) but only contained a series of laminin immunoreactive protein fragments from -120 kDa to -200 kDa (i.e. Figure 12, bands observed between the two arrows). This study determined that a series of laminin protein fragments are present in both human serum and cerebrospinal fluid of Alzheimer's disease, type II diabetes and normal aged patients, whereas intact laminin is only present in human serum. The novel discovery of the laminin fragments in human cerebrospinal fluid suggests that it may be used as a marker to determine the extent of laminin breakdown in the brain during Alzheimer's disease and other brain disorders. Example 9 Identification of a -130 Kilodalton Laminin Protein Fragment in Human Serum of Alzheimer's disease, Type II Diabetes and Normal Aged Patients which Binds Aβ In the next study, Aβ ligand blotting techniques were utilized to identify whether laminin or laminin protein fragments present in human serum bind Aβ. In this study, human serum was obtained from the Alzheimer's disease Research Center at the University of Washington from either living patients who may have had corresponding mini-mental state examinations (where a score of 30 is normal, a score of 15 suggests moderate dementia and a score <10 suggests severe dementia), or from living patients who had subsequently died and were diagnosed at autopsy with Alzheimer's disease (following examination of their brains obtained postmortem). In addition, human serum was obtained from the Diabetes Endocrinology Research Center at the University of Washington. The first six human serum samples (i.e. Figure 13, lanes 1-6) were the same serum samples as indicated in Example 8. In addition, Figure 13 lanes 7-10 consisted of human serum obtained from lane 7) patient #E- a 54 year old male with confirmed type II diabetes, lane 8) patient #5230- a 72 year old female with confirmed moderate Alzheimer's disease who had a mini-mental score of 19, lane 9) patient #E-a 54 year old male with confirmed type II diabetes, and lane 10) patient #F- a 69 year old male with confirmed type II diabetes. For this study, Aβ (1-40) was biotinylated according to the manufacturer's protocol (Pierce, Rockford, IL). For the ligand studies, following SDS-PAGE as described above in Example 8, separated laminin and its fragments present in human serum were transferred to polyvinylidine difluoride membrane (PVDF) using a Mini transblot electrophoresis transfer cell. Electrotransfer was performed at 100V for 2 hours. Following transfer, membranes were rinsed with methanol and dried. The fragment(s) of laminin in human serum involved in binding to AJ3 were then detected by using biotinylated- Aβ (1-40). Blots were probed for 2 hours with 1 μM biotinylated Aβ (1-40) in TTBS. The membranes were then rinsed three times (10 seconds each) with TTBS, probed for 30 minutes with strepavidin alkaline phosphatase conjugate (Vectastain), rinsed again (as described above), and followed by the addition of an alkaline phosphatase substrate solution (Vectastain). Following color development, the reaction was stopped by flushing the membranes with double distilled water. As shown in Figure 13, AJ3 interacted with intact human laminin (arrow) in most samples of human serum. However, it was surprising to note that intact laminin was virtually absent in 2 of the 4 Alzheimer's disease patients serum (Fig. 13, lanes 5 and 8), suggesting that laminin-derived fragments may be important in Alzheimer's disease as a diagnostic marker. The most interesting discovery was that of all the laminin immunoreactive protein fragments found in human serum (i.e -120 kDa to -200 kDa, bands observed between the arrows, Figure 12, lanes 1-7, right side), only a prominent -130 kDa band was found to interact with Aβ (Figure 13, arrowhead). This same prominent band is approximately the same molecular weight of the E8 band generated from mouse laminin following elastase digestion (see Figure 9), and which also contains the globular domain repeats of the laminin A chain. This study therefore determined that besides intact laminin, human serum contains a -130 kDa laminin fragment which binds to Aβ, and may be important for keeping Aβ soluble in biological fluids such as blood. This study also suggests that qualitative and quantitative assessment of laminin fragments in human serum may prove diagnostic for the extent and progression of Alzheimer's disease, type II diabetes and other amyloidoses. Example 10 Identification ofa-130 KilodaltonLaminin Protein Fragment in Human Cerebrospinal Fluid of Alzheimer's disease and Normal Aged Patients which Binds Aβ In the next study, A13 ligand blotting techniques were utilized to identify whether laminin protein fragments (<200 kDa) present in human cerebrospinal fluid bind AJ3. In this study, human cerebrospinal fluid was obtained from the Alzheimer's disease Research Center at the University of Washington from either living aged patients who may have had corresponding mini-mental state examinations (where a score of 30 is normal, a score of 15 suggests moderate Alzheimer's disease and a score <10 suggests moderate Alzheimer's disease), or from living aged patients who had subsequently died and were diagnosed at autopsy with Alzheimer's disease (following examination of their brains obtained postmortem). The following human cerebrospinal fluids were obtained and analyzed as part of this study (depicted in Figure 14, lanes 1-10): 1) patient #65- a 71 yr old male with probable severe Alzheimer's disease as indicated by a mini-mental score of 0; 2) patient #54-a 73 yr old male with probable severe Alzheimer's disease as indicated by a mini-mental score of 8.; 3) patient #6- a normal 64 yr old female who had a mini-mental score of 30; 4) patient #7- a normal 67 yr old male who had a mini-mental score of 30; 5) patient #8- a normal 80 yr old female who had a mini-mental score of 30; 6) patient #9- a normal 67 yr old female who had a mini-mental score of 30; 7) patient #111 IP- a normal 78 yr old female who had a mini-mental score of 30; 8) patient #50-a 66 yr old male patient with probable moderate Alzheimer's disease as indicated by a mini-mental score of 15; 9) patient #52-a 69 yr old male with probable moderate Alzheimer's disease as indicated by a mini-mental score of 16; 10) patient #64-a 64 yr old male with probable severe Alzheimer's disease as indicated by a mini-mental score of 0. Each of these cerebrospinal fluid samples were utilized in this study and represent lanes 1-10 of Figure 14 (in the same order as above). For this study, Aβ ligand blotting was employed as described in Example 9. The fragment(s) of laminin in human cerebrospinal fluid involved in binding to Aβ were detected by using biotinylated-AJ3 (1-40). Blots were probed for 2 hours with 50 nM of biotinylated Aβ (1-40) in TTBS. The rest of the Aβ ligand blotting procedure is as described above in Example 9. As shown in Figure 14, Aβ interacted with laminin fragment bands between - 120 kDa and -200 kDa in most samples of human cerebrospinal fluid. As observed in human serum, most samples of human cerebrospinal fluid also contained a prominent -130 kDa laminin fragment (Figure 14, arrow) which interacted with Aβ. No intact Aβ-binding laminin was found in human cerebrospinal fluid (not shown), as previously demonstrated (Figure 12, Example 8). Again, this same prominent -130 kDa Aβ-binding laminin fragment present in human cerebrospinal fluid is approximately the same molecular weight of the E8 band generated from laminin, and which also contains the globular domain repeats of the laminin A chain. This study therefore determined that human cerebrospinal fluid also contains a - 130 kDa laminin fragment which binds to Aβ, and may be important for keeping Aβ soluble in biological fluids such as cerebrospinal fluid. Further Aspects and Utilizations of the Invention Laminin-Derived Protein Fragments and Polypeptides One therapeutic application of the present invention is to use laminin, laminin protein fragments which bind Aβ or other amyloid proteins, and/or laminin polypeptides derived from amino acid sequencing of the laminin fragments which bind A β (such as the -130 kilodalton protein described herein) or other amyloid proteins, as potent inhibitors of amyloid formation, deposition, accumulation and/or persistence in Alzheimer's disease and other amyloidoses. The amyloid diseases include, but are not limited to, the amyloid associated with Alzheimer's disease and Down's syndrome (wherein the specific amyloid is referred to as beta-amyloid protein or Aβ), the amyloid associated with chronic inflammation, various forms of malignancy and Familial Mediterranean Fever (wherein the specific amyloid is referred to as AA amyloid or inflammation-associated amyloidosis), the amyloid associated with multiple myeloma and other B-cell dyscrasias (wherein the specific amyloid is referred to as AL amyloid), the amyloid associated with type II diabetes (wherein the specific amyloid is referred to as amylin or islet amyloid), the amyloid associated with the prion diseases including Creutzfeldt-Jakob disease, Gerstmann-Straussler syndrome, kuru and animal scrapie (wherein the specific amyloid is referred to as PrP amyloid), the amyloid associated with long-term hemodialysis and carpal tunnel syndrome (wherein the specific amyloid is referred to as beta 2 -microglobulin amyloid), the amyloid associated with senile cardiac amyloid and Familial Amyloidotic Polyneuropathy (wherein the specific amyloid is referred to as transthyretin or prealbumin), and the amyloid associated with endocrine tumors such as medullary carcinoma of the thyroid (wherein the specific amyloid is referred to as variants of procalcitonin). The polypeptides referred to above may be a natural polypeptide, a synthetic polypeptide or a recombinant polypeptide. The fragments, derivatives or analogs of the polypeptides to any laminin fragment referred to herein may be a) one in which one or more of the amino acid residues are substituted with a conserved or non-conserved amino acid residue and such substituted amino acid residue may or may not be encoded by the genetic code, or b) one in which one or more of the amino acid residues includes a substituent group, or c) one in which the mature polypeptide is fused with another compound, such as a compound used to increase the half-life of the polypeptide (for example, polylysine), or d) one in which the additional amino acids are fused to the mature polypeptide, such as a leader or secretory sequence or a sequence which is employed for purification of the mature polypeptide or a proprotein sequence. Such fragments, derivatives and analogs are deemed to be within the scope of the invention. The tertiary structure of proteins refers to the overall 3-dimensional architecture of a polypeptide chain. The complexity of 3-dimensional structure arises from the intrinsic ability of single covalent bonds to be rotated. Rotation about several such bonds in a linear molecule will produce different nonsuperimpossable 3-dimensional arrangements of the atoms that are generally described as conformations. Protein conformation is an essential component of protein-protein, protein-substrate, protein-agonist, protein-antagonist interactions. Changes in the component amino acids of protein sequences can result in changes that have little or no effect on the resultant protein conformation. Conversely, changes in the peptide sequences can have effects on the protein conformation resulting in reduced or increased protein-protein, etc. interactions. Such changes and their effects are generally disclosed in Proteins: Structures and Molecular Properties by Thomas Creightonm W.H. Freeman and Company, New York, 1984 which is hereby incorporated by reference. "Conformation" and "conformation similarity" when used in this specification and claims refers to a polypeptide's ability (or any other organic or inorganic molecule) to assume a given shape, through folding and the like, so that the shape, or conformation, of the molecule becomes an essential part of it's functionality, sometimes to the exclusion of its chemical makeup. It is generally known that in biological processes two conformational similar molecules may be interchangeable in the process, even the chemically different. "Conformational similarity" refers to the latter interchangeability or substitutability. For example, laminin and laminin-derived protein fragments are among the subjects of the invention because they have been shown to bind the Aβ protein and render it inactive in fibril formation; it is contemplated that other molecules that are conformationally similar to laminin, or any claimed laminin fragment or polypeptide, may be substituted in the claimed method to similarly render the Aβ inactive in fibrillogenesis and other amyloid processes. In general it is contemplated that levels of conformational similarity at or above 70% are sufficient to assume homologous functionality in the claimed processes, though reduced levels of conformational similarity may be made to serve as well. Conformational similar levels at or above 90% should provide some level of additional homologue functionality. Thus, one skilled in the art would envisage that changes can be made to the laminin sequence, or fragments or polypeptides thereof, that would increase, decrease or have no effect on the binding of laminin or fragments thereof, to Aβ amyloid. In addition, one skilled in the art would envisage various post-translational modifications such as phosphorylation, glycosylation and the like would alter the binding of laminin, laminin fragments or laminin polypeptides to Aβ amyloid. The polypeptides of the present invention include the polypeptides or fragments of laminin described herein, including but not limited to SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ I D NO: 10 and SEQ ID NO: 11, and fragments thereof, as well as polypeptides which have at least 70% similarity (preferably 70 % identity) and more preferably a 90% similarity (more preferably a 90% identity) to the polypeptides described above. Fragments or portions of the polypeptides or fragments of laminin of the present invention may be employed for producing the corresponding full-length polypeptides by peptide synthesis; therefore, the fragments may be employed as intermediates for producing the full length polypeptides. The polypeptides of the present invention may be a naturally purified product, or a product of chemical synthetic procedures, or produced by recombinant techniques from a prokaryotic or eukaryotic host (for example, by bacterial, yeast, higher plant, insect and mammalian cells in culture). Depending upon the host employed in a recombinant procedure, the polypeptides of the present invention may be glycosylated or may be non-glycosylated. Polypeptides of the invention may also include an initial methionine amino acid residue. Chemical polypeptide synthesis is a rapidly evolving area in the art, and methods of solid phase polypeptide synthesis are well-described in the following references, hereby entirely incorporated by reference (Merrifield, J.Amer.Chem.Soc. 85:2149-2154, 1963; Merrifield. Science 232:341-347. 1986; Fields, Int.J.Polvpeotide Prot.Res. 35, 161, 1990). Recombinant production of laminin polypeptides can be accomplished according to known method steps. Standard reference works seting forth the general principles of recombinant DNA technology include Watson, Molecular Biology of the Gene, Volumes I and II, The Benjamin/Cummings Publishing Company Inc., publisher, Menlo Park, Calif. 1987; Ausubel et al, eds., Current Protocols in Molecular Biology, Wiley Interscience, publisher, New York, N.Y. 1987; 1992; and Sambrook et al, Molecular Cloning: A Laboratory Manual. Second Edition, Cold Spring Harbor Laboratory, publisher, Cold Spring Harbor, N.Y. 1989, the entire contents of which references are herein incorporated by reference. The polypeptides of the present invention may also be utilized as research reagents and materials for discovery of treatments and diagnostics for human diseases. Antibodies Antibodies generated against the polypeptides corresponding to specific sequences recognizing the laminin fragments of the present invention which bind Aβ or other amyloid proteins can be obtained by direct injection of the polypeptides into an animal or by administering the polypeptides to an animal, preferably a nonhuman. The antibody so obtained will then bind the polypeptides itself. In this manner, even a sequence encoding only a fragment of the polypeptides can be used to generate antibodies binding the whole native polypeptides. Such antibodies can then be used to isolate the polypeptides from tissue expressing that polypeptide. Preferred embodiments include, but are not limited to, SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10 and SEQ ID NO: 11, and fragments thereof, as well as polypeptides which have at least 70% similarity (preferably 70 % identity) and more preferably a 90% similarity (more preferably a 90% identity) to the polypeptides described above. The term "antibody" is meant to include polyclonal antibodies, monoclonal antibodies, chimeric antibodies, anti-idiotypic antibodies to antibodies specific for laminin-derived protein fragments or polypeptides of the present invention. Polyclonal antibodies are heterogeneous populations of antibody molecules derived from the sera of animals immunized with an antigen. A monoclonal antibody contains a substantially homogeneous population of antibodies specific to antigens, which population contains substantially similar epitope binding sites. For preparation of monoclonal antibodies, any technique which provides antibodies produced by continuous cell line cultures can be used. Examples include the hybridoma technique (Kohler and Milstein, Nature 256:495-497, 1975), the trioma technique, the human B-cell hybridoma technique (Kozbor et al, Immunology Today 4:72. 1983), and the EBV-hybridoma technique to produce human monoclonal antibodies (Cole et al, in Monoclonal Antibodies and Cancer Therapy, Alan R. Liss, Inc., pp.77-96, 1985). Such antibodies may be of any immunoglobulin class including IgG, IgM, IgE, IgΛ, GILD and any subclass thereof. Chimeric antibodies are molecules different portions of which are derived from different animal species, such as those having variable region derived from a murine monoclonal antibody and a human immunoglobulin constant region, which are primarily used to reduce immunogenicity in application and to increase yields in production. Chimeric antibodies and methods for their production are known in the art (ex. Cabilly et al, Proc.Natl.Acad.Sci.U.S.A 81:3273-3277. 1984; Harlow and Lane: Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory 1988). An anti-idiotypic antibody is an antibody which recognizes unique determinants generally associated with the antigen-binding site of an antibody. An anti-iodiotypic antibody can be prepared by immunizing an animal of the same species and genetic type (e.g., mouse strain) as the source of the monoclonal antibody with the monoclonal antibody to which an anti-iodiotypic antibody is being prepared. The immunized animal will recognize and respond to the idiotypic determinants of the immunizing antibody by producing an antibody to these idiotypic determinants (the anti-idiotypic antibody). See, for example, U.S. Patent No. 4,699,880, which is herein incorporated by reference. The term "antibody" is also meant to include both intact molecules as well as fragments thereof, such as, for example, Fab and F(ab') 2 , which are capable of binding antigen. Fab and F(ab') 2 fragments lack the Fc fragment of intact antibody, clear more rapidly from the circulation, and may have less non-specific tissue binding than an intact antibody (Wahl et al, J. Nucl. Med. 24:316-325, 1983). The antibodies or fragments of antibodies, useful in the present invention may be used to quantitatively or qualitatively detect laminin or laminin-derived fragments in a sample or to detect presence of cells which express a laminin polypeptide of the present invention.This can be accomplished by immunofluorescence techniques employing a fluorescently labeled antibody coupled with light microscopic, flow cytometric or fluorometric detection. One of the ways in which a laminin fragment antibody can be detectably labeled is by linking the same to an enzyme and use in an enzyme immunoassay (EIA). This enzyme, in turn, when later exposed to an appropriate substrate, will react with the substrate in such a manner as to produce a chemical moiety which can be detected, for example, by spectrophotometric, fluorometric, or by visual means. Enzymes which can be used detectably label the antibody include, but are not limited to, malate dehydrogenase, staphylococcal nuclease, delta-5-steroid isomerase, yeast alcohol dehydrogenase, alpha-glycerophosphate dehydrogenase, triose phosphate isomerase, horseradish peroxidase, alkaline phosphatase, asparaginase, glucose oxidase, beta-galactosidase, ribonuclease, urease, catalase, glucose-6-phosphate dehydrogenease, glucoamylase and acetylcholinesterase. The detection can be accomplished by colometric methods which employ a chromogenic substrate for the enzyme. Detection can be accomplished by colometric methods which employ a chromogenic substrate for the enzyme. Detection can also be accomplished by visual comparison of the extent of enzymatic reaction of a substrate with similarly prepared standards (see Harlow and Lane, Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory 1988; Ausubel et al, eds., Current Protocols in Molecular Biology. Wiley Interscience, N.Y. 1987, 1992). Detection may be accomplished using any of a variety of other immunoassays. For example, by radiolabeling of the antibodies or antibody fragments, it is possible to detect R-PTPase through the use of a radioimmunoassay (RIA). A good description of RIA may be found in Laboratory Techniques and Biochemistry in Molecular Biology, by Work et al, North Holland Publishing Company, NY (1978) with particular reference to the chapter entitled "An Introduction to Radioimmune Assay and Related Techniques" by Chard, incorporated entirely by reference herein. The radioactive isotope can be detected by such means as the use of a gamma-counter, a scintillation counter or by autoradiography. It is also possible to label a laminin fragment polypeptide antibody with a fluorescent compound. When the fluorescently labeled antibody is exposed to light of the proper wave length, its presence can then be detected due to fluorescence. Among the most commonly used fluorescent labelling compounds are fluorescein isothiocyanate, rhodamine, phycoerythrin, phycocyanin, allophycocyanin, o-phthaldehyde and fluorescamine, commercially available, e.g., from Molecular Probes, Inc. (Eugene, Oregon, U.S.A.). The antibody can also be detectably labeled using fluorescence emitting metals such as 1B2 EU, or other of the lanthanide series. These metals can be attached to the antibody using such metal groups as diethylenetriamine pentaacetic acid (EDTA). The antibody can also be detectably labeled by coupling it to a chemiluminescent compound. The presence of the chemiluminescent-tagged antibody is then determined by detecting the presence of luminescence that arises during the course of a chemical reaction. Examples of particularly useful chemiluminescent labeling compounds are luminol, isoluminol, theromatic acridinium ester, imidazole, acridinium salt, and oxalate ester. Likewise, a bioluminescent compound may be used to label the antibody of the present invention. Bioluminescence is a type of chemiluminescence found in biological systems in which a catalytic protein increases the efficiency of the chemiluminescent reaction. The presence of a bioluminescent protein is determined by detecting the presence of luminescence. Important bioluminescent compounds for purposes of labeling are luciferin, luciferase and aequorin. The antibodies (or fragments thereof) useful in the present invention may be employed histologically, as in immunofluorescence or immunoelectron microscopy, for in situ detection of a laminin fragment of the present invention. In situ detection may be accomplished by removing a histological specimen from a patient, and providing the labeled antibody of the present invention to such a specimen. The antibody (or fragment) is preferably provided by applying or by overlaying the labeled antibody (or fragment) to a biological sample. Through the use of such a procedure, it is possible to determine not only the presence of a laminin fragment polypeptide but also its distribution on the examined tissue. Using the present invention, those of ordinary skill will readily perceive that any of a wide variety of histological methods (such as staining procedures) can be modified in order to achieve such in situ detection. In accordance with yet a further aspect of the present invention there are provided antibodies against laminin, laminin fragments and/or laminin-derived polypeptides which interact with Aβ or other amyloid proteins, or derivatives thereof. These antibodies can be used for a number of important diagnostic and/or therapeutic applications as described herein. In one aspect of the invention, polyclonal and/or monoclonal antibodies made against laminin, laminin fragments and/or laminin-derived polypeptides which bind Aβ or other amyloid proteins, may be utilized for Western blot analysis (using standard Western blotting techniques knowledgeable to those skilled in the art) to detect the presence of amyloid protein-binding laminin fragments or amyloid protein-binding laminin polypeptides in human tissues and in tissues of other species. Western blot analysis can also be used to determine the apparent size of each amyloid protein-binding laminin fragment. In addition, Western blotting following by scanning densitometry (known to those skilled in the art) can be used to quantitate and compare levels of each of the laminin fragments in tissue samples, biological fluids or biopsies obtained from individuals with specific diseases (such as the amyloid diseases) in comparison to tissue samples, biological fluids or biopsies obtained from normal individuals or controls. Biological fluids, include, but are not limited to, blood, plasma, serum, cerebrospinal fluid, sputum, saliva, urine and stool. In yet another aspect of the invention, polyclonal and/or monoclonal antibodies made against laminin, laminin fragments and/or laminin-derived peptides which bind A13 or other amyloid proteins, can be utilized for immunoprecipitation studies (using standard immunoprecipitation techniques known to one skilled in the art) to detect laminin, laminin fragments and/or laminin-derived peptides which bind Aβ or other amyloid proteins, in tissues, cells and/or biological fluids. Use of the laminin, laminin fragment and/or laminin-derived peptide antibodies for immunoprecipitation studies can also be quantitated to determine relative levels of laminin, laminin fragments and/or laminin-derived peptides which interact with Aβ or other amyloid proteins, in tissues, cells and/or biological fluids. Quantitative immunoprecipitation can be used to compare levels of laminin, laminin fragments and/or laminin amyloid protein-binding peptides in tissue samples, biological fluids or biopsies obtained from individuals with specific diseases (such as the amyloid diseases) in comparison to tissue samples, biological fluids or biopsies obtained from normal individuals or controls. Therapeutic Applications Yet another aspect of the present invention is to make use of laminm, laminm fragments and/or laminin-derived polypeptides as amyloid inhibitory therapeutic agents. The laminin-derived peptide sequences or fragments can be synthesized utilizing standard techniques (le. using an automated synthesizer). Lammin, lammin fragments and/or lamimn-denved polypeptides which bind Aβ or other amyloid proteins, can be used as potential blocking therapeutics for the interaction of lammin in a number of biological processes and diseases (such as in the amyloid diseases described above). In a preferred embodiment, specific peptides made against the amino acid sequence of laminin contained within the -55 kDa laminin fragment (i.e globular repeats within the laminin A chain; SEQ ID NO 3) described in the present invention, may be used to aid in the inhibition of amyloid formation, deposition, accumulation, and /or persistence in a given patient. Likewise, in another preferred embodiment anti-idiotypic antibodies made against laminin, laminin fragments and/or lammin-deπved polypeptides (as described above) may be given to a human patient as potential blocking antibodies to disrupt continued amyloid formation, deposition, accumulation and/or persistence in the given patient Preparations of lammin-deπved polypeptides for parenteral administration include sterile aqueous or non-aqueous solutions, suspensions, and emulsions, which may contain axillary agents or excipients which are known in the art. Pharmaceutical compositions such as tablets, pills, tablets, caplets, soft and hard gelatin capsules, lozenges, sachets, cachets, vegicaps, liquid drops, ehxers, suspensions, emulsions, solutions, syrups, tea bags, aerosols (as a solid or in a liquid medium), suppositories, sterile injectable solutions, sterile packaged powders, can be prepared according to routine methods and are known in the art. In yet another aspect of the invention, lamin , laminin fragments and/or laminm-deπved polypeptides may be used as an effective therapy to block amyloid formation, deposition, accumulation and/or persistence as observed in the amyloid diseases. For example, the invention includes a pharmaceutical composition for use in the treatment of amyloidoses comprising a pharmaceutically effective amount of a laminin, laminin fragment and/or laminin-derived polypeptide anti-idiotypic antibody and a pharmaceutically acceptable carrier. The compositions may contain the laminin, laminin fragments and/or laminin-derived polypeptide anti-idiotypic antibody, either unmodified, conjugated to a potentially therapeutic compound, conjugated to a second protein or protein portion or in a recombinant form (ie. chimeric or bispecific laminin, laminin fragment and/or laminin polypeptide antibody). The compositions may additionally include other antibodies or conjugates. The antibody compositions of the invention can be administered using conventional modes of administration including, but not limited to, topical, intravenous, intra- arterial, intraperitoneal, oral, intralymphatic, intramuscular or intralumbar. Intravenous administration is preferred. The compositions of the invention can be a variety of dosage forms, with the preferred form depending upon the mode of administration and the therapeutic application. Optimal dosage and modes of administration for an individual patient can readily be determined by conventional protocols. Laminin, laminin-derivedprotein fragments, and laminin-derivedpolypeptides, or antibodies of the present invention may be administered by any means that achieve their intended purpose, for example, to treat laminin involved pathologies, such as Alzheimer's disease and other amyloid diseases, or other related pathologies, using a laminin-derived polypeptide described herein, in the form of a pharmaceutical composition. For example, administration of such a composition may be by various parenteral routes such as subcutaneous, intravenous, intradermal, intramuscular, intraperitoneal, intranasal, transdermal or buccal routes. Alternatively, or concurrently, administration may be by the oral route. Parenteral administration can be by bolus injection or by gradual perfusion over time. A preferred mode of using a laminin-derived polypeptide, or antibody pharmaceutical composition of the present invention is by oral administration or intravenous application. A typical regimen for preventing, suppressing or treating laminin-involved pathologies, such as Alzheimer's disease amyloidosis, comprises administration of an effective amount of laminin-derived polypeptides, administered over a period of one or several days, up to and including between one week and about 24 months. It is understood that the dosage of the laminin-derived polypeptides of the present invention administered in vivo or in vitro will be dependent upon the age, sex, health, and weight of the recipient, kind of concurrent treatment, if any, frequency of treatment, and the nature of the effect desired. The most preferred dosage will be tailored to the individual subject, as is understood and determinable by one of skill in the art, without undue experimentation. The total dose required for each treatment may be administered by multiple doses or in a single dose. A laminin-derived polypej)tide may be administered alone or in conjunction with other therapeutics directed to laminin-involved pathologies, such as Alzheimer's disease or amyloid diseases, as described herein. Effective amounts of a laminin-derived polypeptide or composition, which may also include a laminin-fragment derived antibody, are about O.Olμg to about lOOmg/kg body weight, and preferably from about 10 μg to about 50 mg/kg body weight, such as 0.05, 0.07, 0.09, 0.1, 0.5, 0.7, O.9., 1, 2, 5, 10, 20, 25, 30, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95 or 100 mg/kg. Preparations for parenteral administration include sterile aqueous or non-aqueous solutions, suspensions, and emulsions, which may contain axillary agents or excipients which are known in the art. Pharmaceutical compositions comprising at least one laminin-derived polypeptide, such as 1-10 or 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 laminin-derived polypeptides, of the present invention may include all compositions wherein the laminin- derived polypeptide is contained in an amount effective to achieve its intended purpose. In addition to at least one laminin-derived polypeptide, a pharmaceutical composition may contain suitable pharmaceutically acceptable carriers, such as excipients, carriers and/or axillanes which facilitate processing of the active compounds into preparations which can be used pharmaceutically. Pharmaceutical compositions comprising at least one lammin-deπved polypeptide or antibody may also include suitable solutions for administration intravenously, subcutaneously, dermally, orally, mucosally, rectally or may by injection or orally, and contain from about 0 01 to 99 percent, preferably about 20 to 75 percent of active component (I e polypeptide or antibody) together with the excipient. Pharmaceutical compositions for oral administration include pills, tablets, caplets, soft and hard gelatin capsules, lozenges, sachets, cachets, vegicaps, liquid drops, ehxers, suspensions, emulsions, solutions, and syrups. The laminin, laminin-derived protein fragments, and laminin-derived polypeptides for Alzheimer's disease and other central nervous system amyloidoses may be optimized to cross the blood-brain barrier. Methods of introductions include but are not limited to systemic administration, parenteral administration i.e., via an intraperitoneal, intravenous, penoral, subcutaneous, intramuscular, mtraarteπal, intradermal, intramuscular, intranasal, epidural and oral routes. In a preferred embodiment, laminin, laminin-derived protein fragments, and laminin-derived polypeptides may be directly administered to the cerebrospinal fluid by intraventncular injection. In a specific embodiment, it may be desirable to administer laminin, laminin-derived protein fragments, and laminin-derived polypeptides locally to the area or tissue in need of treatment; this may be achieved by, for example, and not by way of limitation, local infusion during surgery, topical application, by injection, by infusion using a cannulae with osmotic pump, by means of a catheter, by means of a suppository, or by means of an implant. In yet another embodiment laminin, laminin-derived protein fragments, and laminin-derived polypeptides may be delivered in a controlled release system, such as an osmotic pump. In yet another embodiment, a controlled release system can be placed in proximity to the therapeutic target, ie. the brain, thus requiring only a fraction of the systemic dose. In yet another aspect of the present invention, peptidomimetic compounds modelled from laminin, laminin fragments and/or laminin-derived polypeptides identified as binding Aβ or other amyloid proteins, may serve as potent inhibitors of amyloid formation, deposition, accumulation and/or persistence in Alzheimer's disease and other amyloidoses. Peptidomimetic modelling is implemented by standard procedures known to those skilled in the art. In yet another aspect of the present invention, compounds that mimic the 3-dimensional Aβ binding site on laminin using computer modelling, may serve as potent inhibitors of amyloid formation, deposition, accumulation and/or persistence in Alzheimer's disease and other amyloidoses. Design and production of such compounds using computer modelling technologies is implemented by standard procedures known to those skilled in the art. Recombinant DNA technology, including human gene therapy, has direct applicability to the laminin proteins and their fragments, of this invention. One skilled in the art can take the peptide sequences disclosed herein and create corresponding nucleotide sequences that code for the corresponding peptide sequences. These sequences can be cloned into vectors such as retroviral vectors, and the like. These vectors can, in turn, be transfected into human cells such as hepatocytes or fibroblasts, and the like. Such transfected cells can be introduced into humans to treat amyloid diseases. Alternatively, the genes can be introduced into the patients directly. The basic techniques of recombinant DNA technology are known to those of ordinary skill in the art and are disclosed in Recombinant DNA Second Edition, Watson, et al., W.H. Freeman and Company, New York, 1992, which is hereby incorporated by reference. Diagnostic Applications Another aspect of the invention is to provide polyclonal and/or monoclonal antibodies against laminin, laminin fragments and/or laminin-derived polypeptides which bind Aβ or other amyloid proteins, which would be utilized to specifically detect laminin, laminin fragments and/or laminin-derived peptides in human tissues and/or biological fluids. In one preferred embodiment, polyclonal or monoclonal antibodies made against a peptide portion or fragment of laminin, can be used to detect and quantify laminin, laminin fragments and/or laminin-derived polypeptides in human tissues and/or biological fluids. Polyclonal and/or monoclonal peptide antibodies can also be utilized to specifically detect laminin fragments and/or laminin-derived polypeptides in human tissues and/or biological fluids. In a preferred embodiment, a polyclonal or monoclonal antibody made specifically against a peptide portion or fragment of -55 kDa elastase-resistent protein which binds Aβ (as described herein), can be used to detect and quantify this laminin fragment in human tissues and/or biological fluids. In another preferred embodiment, a polyclonal or monoclonal antibody made specifically against a peptide portion or fragment of -130 kDa laminin-derived protein which is present in human biological fluids and binds Aβ (as described herein), can be used to detect and quantify this laminin fragment in human tissues and/or biological fluids. Other preferred embodiments include, but are not limited to, making polyclonal or monoclonal antibodies made specifically against a peptide portion or fragment of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10 and SEQ ID NO: 1 1, as well as polypeptides which have at least 70% similarity (preferably 70 % identity) and more preferably a 90% similarity (more preferably a 90% identity) to the polypeptides described above. For detection of laminin fragments and/or laminin-derived polypeptides described above in human tissues, cells, and/or in cell culture, the polyclonal and/or monoclonal antibodies can be utilized using standard immunohistochemical and immunocytochemical techniques, known to one skilled in the art. For detection and quantitation of laminin, laminin fragments and/or laminin-derived polypeptides in biological fluids, including cerebrospinal fluid, blood, plasma, serum, urine, sputum, and/or stool, various types of ELISA assays can be utilized, known to one skilled in the art. An antibody molecule of the present invention may be adapted for utilization in an immunometric assay, also known as a "two-site" or "sandwich" assay. In a typical immunometric assay, a quantity of unlabeled antibody (or fragment of antibody) is bound to a solid support or carrier, and a quantity of detectable labeled soluble antibody is added to permit detection and/or quantitation of the ternary complex formed between solid-phase antibody, antigen, and labeled antibody. In a preferred embodiment, a "sandwich" type of ELISA can be used. Using this preferred method a pilot study is first implemented to determine the quantity of binding of each laminin-fragment monoclonal antibody to microtiter wells. Once this is determined, aliquots (usually in 40 μl of TBS; pH 7.4) of the specific laminin-fragment antibody are allowed to bind overnight to microtiter wells (Maxisorb C plate from Nunc) at 4°C. A series of blank wells not containing any laminin-fragment specific monoclonal antibody are also utilized as controls. The next day, non-bound monoclonal antibody is shaken off the microtiter wells. All of the microtiter wells (including the blank wells) are then blocked by incubating for 2 hours with 300 μl of Tris-buffered saline containing 0.05% Tween-20 (TTBS) plus 2% bovine serum albumin, followed by 5 rinses with TTBS. 200 μl of cerebrospinal fluid, blood, plasma, serum, urine, sputum, and/or stool and/or any other type of biological sample is then diluted (to be determined empirically) in TTBS containing 2% bovine serum albumin and placed in wells (in triplicate) containing bound laminin-fragment antibody (or blank) and incubated for 2 hours at room temperature. The wells are then washed 5 times with TTBS. A second biotinylated-monoclonal antibody against the same laminin-derived fragment (but which is against a different epitope) is then added to each well (usually in 40 μl of TBS; pH 7.4) and allowed to bind for 2 hours at room temperature to any laminin-fragment captured by the first antibody. Following incubation, the wells are washed 5 times with TTBS. Bound materials are then detected by incubating with 100 μl of peroxidase-avidin complex (1:250 dilution in TTBS with 0.1% BSA) for 1 hour on a rotary shaker. After 5 washes with TTBS, a substrate solution (100 μl, OPD-Sigma Fast from Sigma Chemical Co., St. Louis, MO, USA) is added and allowed to develop significant color (usually 8-10 minutes). The reaction is stopped with 50 μl of 4N sulfuric acid and read on a standard spectrophotometer at 490 nm. This ELISA can be utilized to determine differences in specific laminin fragments (and/or Aβ-binding laminin fragments) in biological fluids which can serve as a diagnostic marker to follow the progression on a live patient during the progression of disease (ie. monitoring of amyloid disease as an example). In addition, quantitative changes in laminin fragments can also serve as a prognostic indicator monitoring how a live patient will respond to treatment which targets a given amyloid disease such as Alzheimer's disease. Such assays can be provided in a kit form. A competition assay may also be employed wherein antibodies specific to laminin, laminin fragments and/or laminin-derived polypeptides are attached to a solid support and labelled laminin, laminin fragments and/or laminin-derived polypeptides and a sample derived from a host are passed over the solid support and the amount of label detected attached to the solid support can be correlated to the quantity of laminin, laminin fragments and/or laminin-derived polypeptides in the sample. This standard technique is known to one skilled in the art. Another object of the present invention is to use laminin, laminin fragments and/or laminin-derived polypeptides, in conjunction with laminin, laminin fragment and/or laminin-derived peptide antibodies, in an ELISA assay to detect potential laminin, laminin fragment and/or laminin-derived peptide autoantibodies in human biological fluids. Such a diagnostic assay may be produced in a kit form. In a preferred embodiment, peptides containing the sequences of laminin, laminin-derived fragments and laminin-derived polypeptides as in SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10 and SEQ ID NO: 11, as well as polypeptides which have at least 70% similarity (preferably 70 % identity) and more preferably a 90% similarity (more preferably a 90% identity) to the polypeptides described above, will be used to initially bind to microtiter wells in an ELISA plate. A pilot study is first implemented to determine the quantity of binding of each laminin fragment polypeptide to microtiter wells. Once this is determined, aliquots (usually l-2μg in 40 μl of TBS; pH 7.4) of specific laminin fragment polypeptides (as described herein) are allowed to bind overnight to microtiter wells (Maxisorb C plate from Nunc) at 4°C. All the microtiter wells (including blank wells without the laminin fragment polypeptides) are blocked by incubating for 2 hours with 300 μl of Tris-buffered saline (pH 7.4) with 0.05% Tween-20 (TTBS), containing 2% albumin. This is followed by 5 rinses with TTBS. The patients' biological fluids (i.e., cerebrospinal fluid, blood, plasma, serum, sputum, urine, and/or stool) are then utilized and 200 μl are diluted (to be determined empirically) with TTBS containing 2% bovine serum albumin, and placed in microtiter wells (in triplicate) containing a specific laminin fragment polypeptide or blank wells (which do not contain peptide), and are incubated at 1.5 hours at room temperature. Any autoantibodies present in the biological fluids against the laminin fragment will bind to the substrate bound laminin fragment polypeptide (or fragments thereof). The wells are then rinsed by washing 5 times with TTBS. 100 μl of biotinylated polyclonal goat anti-human IgGs (Sigma Chemical company, St. Louis, MO, USA), diluted 1:500 in TTBS with 0.1% bovine serum albumin, is then aliquoted into each well. Bound materials are detected by incubating with 100 μl of peroxidase-avidin complex (1:250 dilution in TTBS with 0.1% bovine serum albumin) for 1 hour on a rotary shaker. Following 5 washes with TTBS, substrate solution (100 μl, OPD-Sigma Fast from Sigma Chemical Company, St. Louis, MO, USA) is added and allowed to develop significant color (usually 8-10 minutes). The reaction is stopped with 50 μl of 4N sulfuric acid added to each well and read on a standard spectrophotometer at 490 nm. This assay system can be utilized to not only detect the presence of autoantibodies against laminin fragments in biological fluids, but also to monitor the progression of disease by following elevation or diminution of laminin fragment autoantibody levels. It is believed that patients demonstrating excessive laminin fragment formation, deposition, accumulation and/or persistence as may be observed in the amyloid diseases, will also carry autoantibodies against the laminin fragments in their biological fluids. Various ELISA assay systems, knowledgeable to those skilled in the art, can be used to accurately monitor the degree of laminin fragments in biological fluids as a potential diagnostic indicator and prognostic marker for patients during the progression of disease (ie. monitoring of an amyloid disease for example). Such assays can be provided in a kit form. In addition, quantitative changes in laminin fragment autoantibody levels can also serve as a prognostic indicator monitoring how a live patient will respond to treatment which targets a given amyloid disease. Other diagnostic methods utilizing the invention include diagnostic assays for measuring altered levels of laminin, laminin fragments and/or laminin-derived polypeptides in various tissues compared to normal control tissue samples. Assays used to detect levels of laminin, laminin fragments and/or laminin-derived polypeptides in a sample derived from a host are well-known to those skilled in the art and included radioimmunoassays, competitive-binding assays, Western blot analysis and preferably ELISA assays (as described above). Yet another aspect of the present invention is to use the antibodies recognizing laminin, laminin fragments and/or laminin-derived polypeptides for labellings, for example, with a radionucleotide, for radioimaging or radioguided surgery, for in vivo diagnosis, and/or for in vitro diagnosis. In one preferred embodiment, radiolabelled peptides or antibodies made (by one skilled in the art) against laminin, laminin fragments and/or laminin-derived polypeptides may be used as minimally invasive techniques to locate laminin, laminin fragments and/or laminin-derived polypeptides, and concurrent amyloid deposits in a living patient. These same imaging techniques could then be used at regular intervals (ie. every 6 months) to monitor the progression of the amyloid disease by following the specific levels of laminin, laminin fragments and/or laminin-derived polypeptides. Yet another aspect of the present invention is to provide a method which can evaluate a compound's ability to alter (diminish or eliminate) the affinity of a given amyloid protein (as described herein) or amyloid precursor protein, to laminin, laminin-derived fragments or laminin-derived polypeptides. By providing a method of identifying compounds which affect the binding of amyloid proteins, or amyloid precursor proteins to such laminin-derived fragments, the present invention is also useful in identifying compounds which can prevent or impair such binding interaction. Thus, compounds can be identified which specifically affect an event linked with the amyloid formation, amyloid deposition, and/or amyloid persistence condition associated with Alzheimer's disease and other amyloid diseases as described herein. According to one aspect of the invention, to identify for compounds which allow the interaction of amyloid proteins or precursor proteins to laminin-derived fragments or laminin polypeptides, either amyloid or laminin fragments are immobilized, and the other of the two is maintained as a free entity. The free entity is contacted with the immobilized entity in the presence of a test compound for a period of time sufficient to allow binding of the free entity to the immobilized entity, after which the unbound free entity is removed. Using antibodies which recognize the free entity, or other means to detect the presence of bound components, the amount of free entity bound to immobilized entity can be measured. By performing this assay in the presence of a series of known concentrations of test compound and, as a control, the complete absence of test compound, the effectiveness of the test compound to allow binding of free entity to immobilized entity can be determined and a quantitative determination of the effect of the test compound on the affinity of free entity to immobilized entity can be made. By comparing the binding affinity of the amyloid-laminin fragment complex in the presence of a test compound to the binding affinity of the amyloid-laminin fragment complex in the absence of a test compound, the ability of the test compound to modulate the binding can be determined. In the case in which the amyloid is immobilized, it is contacted with free laminin-derived fragments or polypeptides, in the presence of a series of concentrations of test compound. As a control, immobilized amyloid is contacted with free laminin-derived polypeptides, or fragments thereof in the absence of the test compound. Using a series of concentrations of laminin-derived polypeptides, the dissociation constant (K^ or other indicators of binding affinity of amyloid-laminin fragment binding can be determined. In the assay, after the laminin-derived polypeptides or fragments thereof is placed in contact with the immobilized amyloid for a sufficient time to allow binding, the unbound laminin polypeptides are removed. Subsequently, the level of laminin fragment-amyloid binding can be observed. One method uses laminin-derived fragment antibodies, as described in the invention, to detect the amount of specific laminin fragments bound to the amyloid or the amount of free laminin fragments remaining in solution.This information is used to determine first qualitatively whether or not the test compound can allow continued binding between laminin-derived fragments and amyloid. Secondly, the data collected from assays performed using a series of test compounds at various concentrations, can be used to measure quantitatively the binding affinity of the laminin fragment-amyloid complex and thereby determine the effect of the test compound on the affinity between laminin fragments and amyloid. Using this information, compounds can be identified which do not modulate the binding of specific laminin fragments to amyloid and thereby allow the laminin-fragments to reduce the amyloid formation, deposition, accumulation and/or persistence, and the subsequent development and persistence of amyloidosis. Therefore a kit for practicing a method for identifying compounds useful which do not alter laminin, laminin-derived fragments or laminin-derived polypeptides to an immobilized amyloid protein, said kit comprising a) a first container having amyloid protein immobilized upon the inner surface, b) a second container which contains laminin, laminin-derived fragments or laminin-derivedpolypeptides dissolved in solution, c) a third container which contains antibodies specific for said laminin, laminin-derived fragments or laminin-derived polypeptides, said antibodies dissolved in solution, and d) a fourth container which contains labelled antibodies specific for laminin, laminin-derived fragments or laminin-derived polypeptides, said antibodies dissolved in solution. In compliance with the statute, the invention has been described in language more or less specific as to structural features. It is to be understood, however, that the invention is not limited to the specific features shown, since the means and construction shown comprise preferred forms of putting the invention into effect. The invention is, therefore, claimed in any of its forms or modifications within the legitimate and valid scope of the appended claims, appropriately interpreted in accordance with the doctrine of equivalents. SEQUENCE LISTING (1) GENERAL INFORMATION (I) APPLICANTS: Gerardo Castillo and Alan Snow (ii) TITLE OF APPLICATION: Therapeutic and Diagnostic Applications of Laminin and Laminin-Derived Protein Fragments (iii) NUMBER OF SEQUENCES: 11 INFORMATION FOR SEQ ID NO: 1: SEQUENCE CHARACTERISTICS (A) LENGTH: 11 AMINO ACIDS (B) TYPE: AMINO ACID (C) STRANDEDNESS: (D) TOPOLOGY: LINEAR (E) AMINO ACID NUMBERING ACCORDING TO TRANSLATION OF GENEBANK ACCESSION NUMBER P19137 MOLECULAR TYPE: PROTEIN SEQUENCE DESCRIPTION: SEQ ID NO 1: Leu His Arg Glu His Gly Glu Leu Pro Pro Glu 5 10 INFORMATION FOR SEQ ID NO: 2: SEQUENCE CHARACTERISTICS (A) LENGTH: 177 AMINO ACIDS (B) TYPE: AMINO ACID (C) STRANDEDNESS: (D) TOPOLOGY: LINEAR (E) AMINO ACID NUMBERING ACCORDING TO TRANSLATION OF GENEBANK ACCESSION NUMBER P19137 (AMINO ACIDS #2746-2922) MOLECULAR TYPE: PROTEIN SEQUENCE DESCRIPTION: SEQ ID NO 2: Leu Gin Val Gin Leu Ser He Arg Thr Phe Ala Ser Ser Gly Leu He Tyr Tyr Val Ala 1 5 10 15 20 His Gin Asn Gin Met Asp Tyr Ala Thr Leu Gin Leu Gin Glu Gly Arg Leu His Phe Met 25 30 35 40 Phe Asp Leu Gly Lys Gly Arg Thr Lys Val Ser His Pro Ala Leu Leu Ser Asp Gly Lys 45 50 55 60 Trp His Thr Val Lys Thr Glu Tyr He Lys Arg Lys Ala Phe Met Thr Val Asp Gly Gin 65 70 75 80 Glu Ser Pro Ser Val Thr Val Val Gly Asn Ala Thr Thr Leu Asp Val Glu Arg Lys Leu 85 90 95 100 Tyr Leu Gly Gly Leu Pro Ser His Tyr Arg Ala Arg Asn He Gly Thr He Thr His Ser 105 110 115 120 He Pro Ala Cys He Gly Glu He Met Val Asn Gly Gin Gin Leu Asp Lys Asp Arg Pro 125 130 135 140 Leu Ser Ala Ser Ala Val Asp Arg Cys Tyr Val Val Ala Gin Glu Gly Thr Phe Phe Glu 145 150 155 160 Gly Ser Gly Tyr Ala Ala Leu Val Lys Glu Gly Tyr Lys Val Arg Leu Asp 165 170 175 INFORMATION FOR SEQ ID NO: 3: SEQUENCE CHARACTERISTICS (A) LENGTH: 177 AMINO ACIDS (B) TYPE: AMINO ACID (C) STRANDEDNESS: (D) TOPOLOGY: LINEAR (E) AMINO ACID NUMBERING ACCORDING TO TRANSLATION OF GENEBANK ACCESSION NUMBER P25391 (AMINO ACIDS #2737-2913) MOLECULAR TYPE: PROTEIN SEQUENCE DESCRIPTION: SEQ ID NO 3: Leu Ser Val Glu Leu Ser He Arg Thr Phe Ala Ser Ser Gly Leu He Tyr Tyr Met Ala 1 5 10 15 20 His Gin Asn Gin Ala Asp Tyr Ala Val Leu Gin Leu His Gly Gly Arg Leu His Phe Met 25 30 35 40 Phe Asp Leu Gly Lys Gly Arg Thr Lys Val Ser His Pro Ala Leu Leu Ser Asp Gly Lys 45 50 55 60 Trp His Thr Val Lys Thr Asp Tyr Val Lys Arg Lys Gly Phe He Thr Val Asp Gly Arg 65 70 75 80 Glu Ser Pro Met Val Thr Val Val Gly Asp Gly Thr Met Leu Asp Val Glu Gly Leu Phe 85 90 95 100 Tyr Leu Gly Gly Leu Pro Ser Gin Tyr Gin Ala Arg Lys He Gly Asn He Thr His Ser 105 110 115 120 He Pro Ala Cys He Gly Asp Val Thr Val Asn Ser Lys Gin Leu Asp Lys Asp Ser Pro 125 130 135 140 Val Ser Ala Phe Thr Val Asn Arg Cys Tyr Ala Val Ala Gin Glu Gly Thr Tyr Phe Asp 145 150 155 160 Gly Ser Gly Tyr Ala Ala Leu Val Lys Glu Gly Tyr Lys Val Gin Ser Asp 165 170 175 INFORMATION FOR SEQ ID NO: 4: SEQUENCE CHARACTERISTICS (A) LENGTH: 3084 AMINO ACIDS (B) TYPE: AMINO ACID (C) STRANDEDNESS: (D) TOPOLOGY: LINEAR (E) AMINO ACID NUMBERING ACCORDING TO TRANSLATION OF GENEBANK ACCESSION NUMBER P19137 MOLECULAR TYPE: PROTEIN SEQUENCE DESCRIPTION: SEQ ID NO 4: Met Arg Gly Ser Gly Thr Gly Ala Ala Leu Leu Val Leu Leu Ala Ser Val Leu Trp Val 1 5 10 15 20 Thr Val Arg Ser Gin Gin Arg Gly Leu Phe Pro Ala He Leu Asn Leu Ala Thr Asn Ala 25 30 35 40 His He Ser Ala Asn Ala Thr Cys Gly Glu Lys Gly Pro Glu Met Phe Cys Lys Leu Val 45 50 55 60 Glu His Val Pro Gly Arg Pro Val Arg His Ala Gin Cys Arg Val Cys Asp Gly Asn Ser 65 70 75 80 Thr Asn Pro Arg Glu Arg His Pro He Ser His Ala He Asp Gly Thr Asn Asn Trp Trp 85 90 95 100 Gin Ser Pro Ser He Gin Asn Gly Arg Glu Tyr His Trp Val Thr Val Thr Leu Asp Leu 105 110 115 120 Arg Gin Val Phe Gin Val Ala Tyr He He He Lys Ala Ala Asn Ala Pro Arg Pro Gly 125 130 135 140 Asn Trp He Leu Glu Arg Ser Val Asp Gly Val Lys Phe Lys Pro Trp Gin Tyr Tyr Ala 145 150 155 160 Val Ser Asp Thr Glu Cys Leu Thr Arg Tyr Lys He Thr Pro Arg Arg Gly Pro Pro Thr 165 170 175 180 Tyr Arg Ala Asp Asn Glu Val He Cys Thr Ser Tyr Tyr Ser Lys Leu Val Pro Leu Glu 185 190 195 200 His Gly Glu He His Thr Ser Leu He Asn Gly Arg Pro Ser Ala Asp Asp Pro Ser Pro 205 210 215 220 Gin Leu Leu Glu Phe Thr Ser Ala Arg Tyr He Arg Leu Arg Leu Gin Arg He Arg Thr 225 230 235 240 Leu Asn Ala Asp Leu Met Thr Leu Ser His Arg Asp Leu Arg Asp Leu Asp Pro He Val 245 250 255 260 Thr Arg Arg Tyr Tyr Tyr Ser He Lys Asp He Ser Val Gly Gly Met Cys He Cys Tyr 265 270 275 280 Gly His Ala Ser Ser Cys Pro Trp Asp Glu Glu Ala Lys Gin Leu Gin Cys Gin Cys Glu 285 290 295 300 His Asn Thr Cys Gly Glu Ser Cys Asp Arg Cys Cys Pro Gly Tyr His Gin Gin Pro Trp 305 310 315 320 Arg Pro Gly Thr He Ser Ser Gly Asn Glu Cys Glu Glu Cys Asn Cys His Asn Lys Ala 325 330 335 340 Lys Asp Cys Tyr Tyr Asp Ser Ser Val Ala Lys Glu Arg Arg Ser Leu Asn Thr Ala Gly 345 350 355 360 Gin Tyr Ser Gly Gly Gly Val Cys Val Asn Cys Ser Gin Asn Thr Thr Gly He Asn Cys 365 370 375 380 Glu Thr Cys He Asp Gin Tyr Tyr Arg Pro His Lys Val Ser Pro Tyr Asp Asp His Pro 385 390 395 400 Cys Arg Pro Cys Asn Cys Asp Pro Val Gly Ser Leu Ser Ser Val Cys He Lys Asp Asp 405 410 415 420 Arg His Ala Asp Leu Ala Asn Gly Lys Trp Pro Gly Gin Cys Pro Cys Arg Lys Gly Tyr 425 430 435 440 Ala Gly Asp Lys Cys Asp Arg Cys Gin Phe Gly Tyr Arg Gly Phe Pro Asn Cys He Pro 445 450 455 460 Cys Asp Cys Arg Thr Val Gly Ser Leu Asn Glu Asp Pro Cys He Glu Pro Cys Leu Cys 465 470 475 480 Lys Lys Asn Val Glu Gly Lys Asn Cys Asp Arg Cys Lys Pro Gly Phe Tyr Asn Leu Lys 485 490 495 500 Glu Arg Asn Pro Glu Gly Cys Ser Glu Cys Phe Cys Phe Gly Val Ser Gly Val Cys Asp 505 510 515 520 Ser Leu Thr Trp Ser He Ser Gin Val Thr Asn Met Ser Gly Trp Leu Val Thr Asp Leu 525 530 535 540 Met Ser Thr Asn Lys He Arg Ser Gin Gin Asp Val Leu Gly Gly His Arg Gin He Ser 545 550 555 560 He Asn Asn Thr Ala Val Met Gin Arg Leu Thr Ser Thr Tyr Tyr Trp Ala Ala Pro Glu 565 570 575 580 Ala Tyr Leu Gly Asn Lys Leu Thr Ala Phe Gly Gly Phe Leu Lys Tyr Thr Val Ser Tyr 585 590 595 600 Asp He Pro Val Glu Thr Val Asp Ser Asp Leu Met Ser His Ala Asp He He He Lys 605 610 615 620 Gly Asn Gly Leu Thr He Ser Thr Arg Ala Glu Gly Leu Ser Leu Gin Pro Tyr Glu Glu 625 630 635 640 Tyr Phe Asn Val Val Arg Leu Val Pro Glu Asn Phe Arg Asp Phe Asn Thr Arg Arg Glu 645 650 655 660 He Asp Arg Asp Gin Leu Met Thr Val Leu Ala Asn Val Thr His Leu Leu He Arg Ala 665 670 675 680 Asn Tyr Asn Ser Ala Lys Met Ala Leu Tyr Arg Leu Asp Ser Val Ser Leu Asp He Ala 685 690 695 700 Ser Pro Asn Ala He Asp Leu Ala Val Ala Ala Asp Val Glu His Cys Glu Cys Pro Gin 705 710 715 720 Gly Tyr Thr Gly Thr Ser Cys Glu Ala Cys Leu Pro Gly Tyr Tyr Arg Val Asp Gly He 725 730 735 740 Leu Phe Gly Gly He Cys Gin Pro Cys Glu Cys His Gly His Ala Ser Glu Cys Asp He 745 750 755 760 His Gly He Cys Ser Val Cys Thr His Asn Thr Thr Gly Asp His Cys Glu Gin Cys Leu 765 770 775 780 Pro Gly Phe Tyr Gly Thr Pro Ser Arg Gly Thr Pro Gly Asp Cys Gin Pro Cys Ala Cys 785 790 795 800 Pro Leu Ser He Asp Ser Asn Asn Phe Ser Pro Thr Cys His Leu Thr Asp Gly Glu Glu 805 810 815 820 Val Val Cys Asp Gin Cys Ala Pro Gly Tyr Ser Gly Ser Trp Cys Glu Arg Cys Ala Asp 825 830 835 840 Gly Tyr Tyr Gly Asn Pro Thr Val Pro Gly Gly Thr Cys Val Pro Cys Asn Cys Ser Gly 845 850 855 860 Asn Val Asp Pro Leu Glu Ala Gly His Cys Asp Ser Val Thr Gly Glu Cys Leu Lys Cys 865 870 875 880 Leu Trp Asn Thr Asp Gly Ala His Cys Glu Arg Cys Ala Asp Gly Phe Tyr Gly Asp Ala 885 890 895 900 Val Thr Ala Lys Asn Cys Arg Ala Cys Asp Cys His Glu Asn Gly Ser Leu Ser Gly Val 905 910 915 920 Cys His Leu Glu Thr Gly Leu Cys Asp Cys Lys Pro His Val Thr Gly Gin Gin Cys Asp 925 930 935 940 Gin Cys Leu Ser Gly Tyr Tyr Gly Leu Asp Thr Gly Leu Gly Cys Val Pro Cys Asn Cys 945 950 955 960 Ser Val Glu Gly Ser Val Ser Asp Asn Cys Thr Glu Glu Gly Gin Cys His Cys Gly Pro 965 970 975 980 Gly Val Ser Gly Lys Gin Cys Asp Arg Cys Ser His Gly Phe Tyr Ala Phe Gin Asp Gly 985 990 995 1000 Gly Cys Thr Pro Cys Asp Cys Ala His Thr Gin Asn Asn Cys Asp Pro Ala Ser Gly Glu 1005 1010 1015 1020 Cys Leu Cys Pro Pro His Thr Gin Gly Leu Lys Cys Glu Glu Cys Glu Glu Ala Tyr Trp 1025 1030 1035 1040 Gly Leu Asp Pro Glu Gin Gly Cys Gin Ala Cys Asn Cys Ser Ala Val Gly Ser Thr Ser 1045 1050 1055 1060 Ala Gin Cys Asp Val Leu Ser Gly His Cys Pro Cys Lys Lys Gly Phe Gly Gly Gin Ser 1065 1070 1075 1080 Cys His Gin Cys Ser Leu Gly Tyr Arg Ser Phe Pro Asp Cys Val Pro Cys Gly Cys Asp 1085 1090 1095 1100 Leu Arg Gly Thr Leu Pro Asp Thr Cys Asp Leu Glu Gin Gly Leu Cys Ser Cys Ser Glu 1105 1110 1115 1120 Asp Ser Gly Thr Cys Ser Cys Lys Glu Asn Val Val Gly Pro Gin Cys Ser Lys Cys Gin 1125 1130 1135 1140 Ala Gly Thr Phe Ala Leu Arg Gly Asp Asn Pro Gin Gly Cys Ser Pro Cys Phe Cys Phe 1145 1150 1155 1160 Gly Leu Ser Gin Leu Cys Ser Glu Leu Glu Gly Tyr Val Arg Thr Leu He Thr Leu Ala 1165 1170 1175 1180 Ser Asp Gin Pro Leu Leu His Val Val Ser Gin Ser Asn Leu Lys Gly Thr He Glu Gly 1185 1190 1195 1200 Val His Phe Gin Pro Pro Asp Thr Leu Leu Asp Ala Glu Ala Val Arg Gin His He Tyr 1205 1210 1215 1220 Ala Glu Pro Phe Tyr Trp Arg Leu Pro Lys Gin Phe Gin Gly Asp Gin Leu Leu Ala Tyr 1225 1230 1235 1240 Gly Gly Lys Leu Gin Tyr Ser Val Ala Phe Tyr Ser Thr Leu Gly Thr Gly Thr Ser Asn 1245 1250 1255 1260 Tyr Glu Pro Gin Val Leu He Lys Gly Gly Arg Ala Arg Lys His Val He Tyr Met Asp 1265 1270 1275 1280 Ala Pro Ala Pro Glu Asn Gly Val Arg Gin Asp Tyr Glu Val Gin Met Lys Glu Glu Phe 1285 1290 1295 1300 Trp Lys Tyr Phe Asn Ser Val Ser Glu Lys His Val Thr His Ser Asp Phe Met Ser Val 1305 1310 1315 1320 Leu Ser Asn He Asp Tyr He Leu He Lys Ala Ser Tyr Gly Gin Gly Leu Gin Gin Ser 1325 1330 1335 1340 Arg He Ala Asn He Ser Met Glu Val Gly Arg Lys Ala Val Glu Leu Pro Ala Glu Gly 1345 1350 1355 1360 Glu Ala Ala Leu Leu Leu Glu Leu Cys Val Cys Pro Pro Gly Thr Ala Gly His Ser Cys 1365 1370 1375 1380 Gin Asp Cys Ala Pro Gly Tyr Tyr Arg Glu Lys Leu Pro Glu Ser Gly Gly Arg Gly Pro 1385 1390 1395 1400 Arg Pro Leu Leu Ala Pro Cys Val Pro Cys Asn Cys Asn Asn His Ser Asp Val Cys Asp 1405 1410 1415 1420 Pro Glu Thr Gly Lys Cys Leu Ser Cys Arg Asp His Thr Ser Gly Asp His Cys Glu Leu 1425 1430 1435 1440 Cys Ala Ser Gly Tyr Tyr Gly Lys Val Thr Gly Leu Pro Gly Asp Cys Thr Pro Cys Thr 1445 1450 1455 1460 Cys Pro His His Pro Pro Phe Ser Phe Ser Pro Thr Cys Val Val Glu Gly Asp Ser Asp 1465 1470 1475 1480 Phe Arg Cys Asn Ala Cys Leu Pro Gly Tyr Glu Gly Gin Tyr Cys Glu Arg Cys Ser Ala 1485 1490 1495 1500 Gly Tyr His Gly Asn Pro Arg Ala Ala Gly Gly Ser Cys Gin Thr Cys Asp Cys Asn Pro 1505 1510 1515 1520 Gin Gly Ser Val His Ser Asp Cys Asp Arg Ala Ser Gly Gin Cys Val Cys Lys Pro Gly 1525 1530 1535 1540 Ala Thr Gly Leu His Cys Glu Lys Cys Leu Pro Arg His He Leu Met Glu Ser Asp Cys 1545 1550 1555 1560 Val Ser Cys Asp Asp Asp Cys Val Gly Pro Leu Leu Asn Asp Leu Asp Ser Val Gly Asp 1565 1570 1575 1580 Ala Val Leu Ser Leu Asn Leu Thr Gly Val Ser Pro Ala Pro Tyr Gly He Leu Glu Asn 1585 1590 1595 1600 Leu Glu Asn Thr Thr Lys Tyr Phe Gin Arg Tyr Leu He Lys Glu Asn Ala Lys Lys He 1605 1610 1615 1620 Arg Ala Glu He Gin Leu Glu Gly He Ala Glu Gin Thr Glu Asn Leu Gin Lys Glu Leu 1625 1630 1635 1640 Thr Arg Val Leu Ala Arg His Gin Lys Val Asn Ala Glu Met Glu Arg Thr Ser Asn Gly 1645 1650 1655 1660 Thr Gin Ala Leu Ala Thr Phe He Glu Gin Leu His Ala Asn He Lys Glu He Thr Glu 1665 1670 1675 1680 Lys Val Ala Thr Leu Asn Gin Thr Ala Arg Lys Asp Phe Gin Pro Pro Val Ser Ala Leu 1685 1690 1695 1700 Gin Ser Met His Gin Asn He Ser Ser Leu Leu Gly Leu He Lys Glu Arg Asn Phe Thr 1705 1710 1715 1720 Glu Met Gin Gin Asn Ala Thr Leu Glu Leu Lys Ala Ala Lys Asp Leu Leu Ser Arg He 1725 1730 1735 1740 Gin Lys Arg Phe Gin Lys Pro Gin Glu Lys Leu Lys Ala Leu Lys Glu Ala Asn Ser Leu 1745 1750 1755 1760 Leu Ser Asn His Ser Glu Lys Leu Gin Ala Ala Glu Glu Leu Leu Lys Glu Ala Gly Ser 1765 1770 1775 1780 Lys Thr Gin Glu Ser Asn Leu Leu Leu Leu Leu Val Lys Ala Asn Leu Lys Glu Glu Phe 1785 1790 1795 1800 Gin Glu Lys Lys Leu Arg Val Gin Glu Glu Gin Asn Val Thr Ser Glu Leu He Ala Lys 1805 1810 1815 1820 Gly Arg Glu Trp Val Asp Ala Ala Gly Thr His Thr Ala Ala Ala Gin Asp Thr Leu Thr 1825 1830 1835 1840 Gin Leu Glu His His Arg Asp Glu Leu Leu Leu Trp Ala Arg Lys He Arg Ser His Val 1845 1850 1855 1860 Asp Asp Leu Val Met Gin Met Ser Lys Arg Arg Ala Arg Asp Leu Val His Arg Ala Glu 1865 1870 1875 1880 Gin His Ala Ser Glu Leu Gin Ser Arg Ala Gly Ala Leu Asp Arg Asp Leu Glu Asn Val 1885 1890 1895 1900 Arg Asn Val Ser Leu Asn Ala Thr Ser Ala Ala His Val His Ser Asn He Gin Thr Leu 1905 1910 1915 1920 Thr Glu Glu Ala Glu Met Leu Ala Ala Asp Ala His Lys Thr Ala Asn Lys Thr Asp Leu 1925 1930 1935 1940 He Ser Glu Ser Leu Ala Ser Arg Gly Lys Ala Val Leu Gin Arg Ser Ser Arg Phe Leu 1945 1950 1955 1960 Lys Glu Ser Val Gly Thr Arg Arg Lys Gin Gin Gly He Thr Met Lys Leu Asp Glu Leu 1965 1970 1975 1980 Lys Asn Leu Thr Ser Gin Phe Gin Glu Ser Val Asp Asn He Thr Lys Gin Ala Asn Asp 1985 1990 1995 2000 Ser Leu Ala Met Leu Arg Glu Ser Pro Gly Gly Met Arg Glu Lys Gly Arg Lys Ala Arg 2005 2010 2015 2020 Glu Leu Ala Ala Ala Ala Asn Glu Ser Ala Val Lys Thr Leu Glu Asp Val Leu Ala Leu 2025 2030 2035 2040 Ser Leu Arg Val Phe Asn Thr Ser Glu Asp Leu Ser Arg Val Asn Ala Thr Val Gin Glu 2045 2050 2055 2060 Thr Asn Asp Leu Leu His Asn Ser Thr Met Thr Thr Leu Leu Ala Gly Arg Lys Met Lys 2065 2070 2075 2080 Asp Met Glu Met Gin Ala Asn Leu Leu Leu Asp Arg Leu Lys Pro Leu Lys Thr Leu Glu 2085 2090 2095 2100 Glu Asn Leu Ser Arg Asn Leu Ser Glu He Lys Leu Leu He Ser Arg Ala Arg Lys Gin 2105 2110 2115 2120 Ala Ala Ser He Lys Val Ala Val Ser Ala Asp Arg Asp Cys He Arg Ala Tyr Gin Pro 2125 2130 2135 2140 Gin Thr Ser Ser Thr Asn Tyr Asn Thr Leu He Leu Asn Val Lys Thr Gin Glu Pro Asp 2145 2150 2155 2160 Asn Leu Leu Phe Tyr Leu Gly Ser Ser Ser Ser Ser Asp Phe Leu Ala Val Glu Met Arg 2165 2170 2175 2180 Arg Gly Lys Val Ala Phe Leu Trp Asp Leu Gly Ser Gly Ser Thr Arg Leu Glu Phe Pro 2185 2190 2195 2200 Glu Val Ser He Asn Asn Asn Arg Trp His Ser He Tyr He Thr Arg Phe Gly Asn Met 2205 2210 2215 2220 Gly Ser Leu Ser Val Lys Glu Ala Ser Ala Ala Glu Asn Pro Pro Val Arg Thr Ser Lys 2225 2230 2235 2240 Ser Pro Gly Pro Ser Lys Val Leu Asp He Asn Asn Ser Thr Leu Met Phe Val Gly Gly 2245 2250 2255 2260 Leu Gly Gly Gin He Lys Lys Ser Pro Ala Val Lys Val Thr His Phe Lys Gly Cys Met 2265 2270 2275 2280 Gly Glu Ala Phe Leu Asn Gly Lys Ser He Gly Leu Trp Asn Tyr He Glu Arg Glu Gly 2285 2290 2295 2300 Lys Cys Asn Gly Cys Phe Gly Ser Ser Gin Asn Glu Asp Ser Ser Phe His Phe Asp Gly 2305 2310 2315 2320 Ser Gly Tyr Ala Met Val Glu Lys Thr Leu Arg Pro Thr Val Thr Gin He Val He Leu 2325 2330 2335 2340 Phe Ser Thr Phe Ser Pro Asn Gly Leu Leu Phe Tyr Leu Ala Ser Asn Gly Thr Lys Asp 2345 2350 2355 2360 Phe Leu Ser He Glu Leu Val Arg Gly Arg Val Lys Val Met Val Asp Leu Gly Ser Gly 2365 2370 2375 2380 Pro Leu Thr Leu Met Thr Asp Arg Arg Tyr Asn Asn Gly Thr Trp Tyr Lys He Ala Phe 2385 2390 2395 2400 Gin Arg Asn Arg Lys Gin Gly Leu Leu Ala Val Phe Asp Ala Tyr Asp Thr Ser Asp Lys 2405 2410 2415 2420 Glu Thr Lys Gin Gly Glu Thr Pro Gly Ala Ala Ser Asp Leu Asn Arg Leu Glu Lys Asp 2425 2430 2435 2440 Leu He Tyr Val Gly Gly Leu Pro His Ser Lys Ala Val Arg Lys Gly Val Ser Ser Arg 2445 2450 2455 2460 Ser Tyr Val Gly Cys He Lys Asn Leu Glu He Ser Arg Ser Thr Phe Asp Leu Leu Arg 2465 2470 2475 2480 Asn Ser Tyr Gly Val Arg Lys Gly Cys Ala Leu Glu Pro He Gin Ser Val Ser Phe Leu 2485 2490 2495 2500 Arg Gly Gly Tyr Val Glu Met Pro Pro Lys Ser Leu Ser Pro Glu Ser Ser Leu Leu Ala 2505 2510 2515 2520 Thr Phe Ala Thr Lys Asn Ser Ser Gly He Leu Leu Val Ala Leu Gly Lys Asp Ala Glu 2525 2530 2535 2540 Glu Ala Gly Gly Ala Gin Ala His Val Pro Phe Phe Ser He Met Leu Leu Glu Gly Arg 2545 2550 2555 2560 He Glu Val His Val Asn Ser Gly Asp Gly Thr Ser Leu Arg Lys Ala Leu Leu His Ala 2565 2570 2575 2580 Pro Thr Gly Ser Tyr Ser Asp Gly Gin Glu His Ser He Ser Leu Val Arg Asn Arg Arg 2585 2590 2595 2600 Val He Thr He Gin Val Asp Glu Asn Ser Pro Val Glu Met Lys Leu Gly Pro Leu Thr 2605 2610 2615 2620 Glu Gly Lys Thr He Asp He Ser Asn Leu Tyr He Gly Gly Leu Pro Glu Asp Lys Ala 2625 2630 2635 2640 Thr Pro Met Leu Lys Met Arg Thr Ser Phe His Gly Cys He Lys Asn Val Val Leu Asp 2645 2650 2655 2660 Ala Gin Leu Leu Asp Phe Thr His Ala Thr Gly Ser Glu Gin Val Glu Leu Asp Thr Cys 2665 2670 2675 2680 Leu Leu Ala Glu Glu Pro Met Gin Ser Leu His Arg Glu His Gly Glu Leu Pro Pro Glu 2685 2690 2695 2700 Pro Pro Thr Leu Pro Gin Pro Glu Leu Cys Ala Val Asp Thr Ala Pro Gly Tyr Val Ala 2705 2710 2715 2720 Gly Ala His Gin Phe Gly Leu Ser Gin Asn Ser His Leu Val Leu Pro Leu Asn Gin Ser 2725 2730 2735 2740 Asp Val Arg Lys Arg Leu Gin Val Gin Leu Ser He Arg Thr Phe Ala Ser Ser Gly Leu 2745 2750 2755 2760 He Tyr Tyr Val Ala His Gin Asn Gin Met Asp Tyr Ala Thr Leu Gin Leu Gin Glu Gly 2765 2770 2775 2780 Arg Leu His Phe Met Phe Asp Leu Gly Lys Gly Arg Thr Lys Val Ser His Pro Ala Leu 2785 2790 2795 2800 Leu Ser Asp Gly Lys Trp His Thr Val Lys Thr Glu Tyr He Lys Arg Lys Ala Phe Met 2805 2810 2815 2820 Thr Val Asp Gly Gin Glu Ser Pro Ser Val Thr Val Val Gly Asn Ala Thr Thr Leu Asp 2825 2830 2835 2840 Val Glu Arg Lys Leu Tyr Leu Gly Gly Leu Pro Ser His Tyr Arg Ala Arg Asn He Gly 2845 2850 2855 2860 Thr He Thr His Ser He Pro Ala Cys He Gly Glu He Met Val Asn Gly Gin Gin Leu 2865 2870 2875 2880 Asp Lys Asp Arg Pro Leu Ser Ala Ser Ala Val Asp Arg Cys Tyr Val Val Ala Gin Glu 2885 2890 2895 2900 Gly Thr Phe Phe Glu Gly Ser Gly Tyr Ala Ala Leu Val Lys Glu Gly Tyr Lys Val Arg 2905 2910 2915 2920 Leu Asp Leu Asn He Thr Leu Glu Phe Arg Thr Thr Ser Lys Asn Gly Val Leu Leu Gly 2925 2930 2935 2940 He Ser Ser Ala Lys Val Asp Ala He Gly Leu Glu He Val Asp Gly Lys Val Leu Phe 2945 2950 2955 2960 His Val Asn Asn Gly Ala Gly Arg He Thr Ala Thr Tyr Gin Pro Arg Ala Ala Arg Ala 2965 2970 2975 2980 Leu Cys Asp Gly Lys Trp His Thr Leu Gin Ala His Lys Ser Lys His Arg He Val Leu 2985 2990 2995 3000 Thr Val Asp Gly Asn Ser Val Arg Ala Glu Ser Pro His Thr His Ser Thr Ser Ala Asp 3005 3010 3015 3020 Thr Asn Asp Pro He Tyr Val Gly Gly Tyr Pro Ala His He Lys Gin Asn Cys Leu Ser 3025 3030 3035 3040 Ser Arg Ala Ser Phe Arg Gly Cys Val Arg Asn Leu Arg Leu Ser Arg Gly Ser Gin Val 3045 3050 3055 3060 Gin Ser Leu Asp Leu Ser Arg Ala Phe Asp Leu Gin Gly Val Phe Pro His Ser Cys Pro 3065 3070 3075 3080 Gly Pro Glu Pro INFORMATION FOR SEQ ID NO: 5: SEQUENCE CHARACTERISTICS (A) LENGTH: 3075 AMINO ACIDS (B) TYPE: AMINO ACID (C) STRANDEDNESS: (D) TOPOLOGY: LINEAR (E) AMINO ACID NUMBERING ACCORDING TO TRANSLATION OF GENEBANK ACCESSION NUMBER P25391 MOLECULAR TYPE: PROTEIN SEQUENCE DESCRIPTION: SEQ ID NO 5: Met Arg Gly Gly Val Leu Leu Val Leu Leu Leu Cys Val Ala Ala Gin Cys Arg Gin Arg 1 5 10 15 20 Gly Leu Phe Pro Ala He Leu Asn Leu Ala Ser Asn Ala His He Ser Thr Asn Ala Thr 25 30 35 40 Cys Gly Glu Lys Gly Pro Glu Met Phe Cys Lys Leu Val Glu His Val Pro Gly Arg Pro 45 50 55 60 Val Arg Asn Pro Gin Cys Arg He Cys Asp Gly Asn Ser Ala Asn Pro Arg Glu Arg His 65 70 75 80 Pro He Ser His Ala He Asp Gly Thr Asn Asn Trp Trp Gin Ser Pro Ser He Gin Asn 85 90 95 100 Gly Arg Glu Tyr His Trp Val Thr He Thr Leu Asp Leu Arg Gin Val Phe Gin Val Ala 105 110 115 120 Tyr Val He He Lys Ala Ala Asn Ala Pro Arg Pro Gly Asn Trp He Leu Glu Arg Ser 125 130 135 140 Leu Asp Gly Thr Thr Phe Ser Pro Trp Gin Tyr Tyr Ala Val Ser Asp Ser Glu Cys Leu 145 150 155 160 Ser Arg Tyr Asn He Thr Pro Arg Arg Gly Pro Pro Thr Tyr Arg Ala Asp Asp Glu Val 165 170 175 180 He Cys Thr Ser Tyr Tyr Ser Arg Leu Val Pro Leu Glu His Gly Glu He His Thr Ser 185 190 195 200 Leu He Asn Gly Arg Pro Ser Ala Asp Asp Leu Ser Pro Lys Leu Leu Glu Phe Thr Ser 205 210 215 220 Ala Arg Tyr He Arg Leu Arg Leu Gin Arg He Arg Thr Leu Asn Ala Asp Leu Met Thr 225 230 235 240 Leu Ser His Arg Glu Pro Lys Glu Leu Asp Pro He Val Thr Arg Arg Tyr Tyr Tyr Ser 245 250 255 260 He Lys Asp He Ser Val Gly Gly Met Cys He Cys Tyr Gly His Ala Ser Ser Cys Pro 265 270 275 280 Trp Asp Glu Thr Thr Lys Lys Leu Gin Cys Gin Cys Glu His Asn Thr Cys Gly Glu Ser 285 290 295 300 Cys Asn Arg Cys Cys Pro Gly Tyr His Gin Gin Pro Trp Arg Pro Gly Thr Val Ser Ser 305 310 315 320 Gly Asn Thr Cys Glu Ala Cys Asn Cys His Asn Lys Ala Lys Asp Cys Tyr Tyr Asp Glu 325 330 335 340 Ser Val Ala Lys Gin Lys Lys Ser Leu Asn Thr Ala Gly Gin Phe Arg Gly Gly Gly Val 345 350 355 360 Cys He Asn Cys Leu Gin Asn Thr Met Gly He Asn Cys Glu Thr Cys He Asp Gly Tyr 365 370 375 380 Tyr Arg Pro His Lys Val Ser Pro Tyr Glu Asp Glu Pro Cys Arg Pro Cys Asn Cys Asp 385 390 395 400 Pro Val Gly Ser Leu Ser Ser Val Cys He Lys Asp Asp Leu His Ser Asp Leu His Asn 405 410 415 420 Gly Lys Gin Pro Gly Gin Cys Pro Cys Lys Glu Gly Tyr Thr Gly Glu Lys Cys Asp Arg 425 430 435 440 Cys Gin Leu Gly Tyr Lys Asp Tyr Pro Thr Cys Val Ser Cys Gly Cys Asn Pro Val Gly 445 450 455 460 Ser Ala Ser Asp Glu Pro Cys Thr Gly Pro Cys Val Cys Lys Glu Asn Val Glu Gly Lys 465 470 475 480 Ala Cys Asp Arg Cys Lys Pro Gly Phe Tyr Asn Leu Lys Glu Lys Asn Pro Arg Gly Cys 485 490 495 500 Ser Glu Cys Phe Cys Phe Gly Val Ser Asp Val Cys Ser Ser Leu Ser Trp Pro Val Gly 505 510 515 520 Gin Val Asn Ser Met Ser Gly Trp Leu Val Thr Asp Leu He Ser Pro Arg Lys He Pro 525 530 535 540 Ser Gin Gin Asp Ala Leu Gly Gly Arg His Gin Val Ser He Asn Asn Thr Ala Val Met 545 550 555 560 Gin Arg Leu Ala Pro Lys Tyr Tyr Trp Ala Ala Pro Glu Ala Tyr Leu Gly Asn Lys Leu 565 570 575 580 Thr Ala Phe Gly Gly Phe Leu Lys Tyr Thr Val Ser Tyr Asp He Pro Val Glu Thr Val 585 590 595 600 Asp Ser Asn Leu Met Ser His Ala Asp Val He He Lys Gly Asn Gly Leu Thr Leu Ser 605 610 615 620 Thr Gin Ala Glu Gly Leu Ser Leu Gin Pro Tyr Glu Glu Tyr Leu Asn Val Val Arg Leu 625 630 635 640 Val Pro Glu Asn Phe Gin Asp Phe His Ser Lys Arg Gin He Asp Arg Asp Gin Leu Met 645 650 655 660 Thr Val Leu Ala Asn Val Thr His Leu Leu He Arg Ala Thr Tyr Asn Ser Ala Lys Met 665 670 675 680 Ala Leu Tyr Arg Leu Glu Ser Val Ser Leu Asp He Ala Ser Ser Asn Ala He Asp Leu 685 690 695 700 Val Val Ala Ala Asp Val Glu His Cys Glu Cys Pro Gin Gly Tyr Thr Gly Thr Ser Cys 705 710 715 720 Glu Ser Cys Leu Ser Gly Tyr Tyr Arg Val Asp Gly He Leu Phe Gly Gly He Cys Gin 725 730 735 740 Pro Cys Glu Cys His Gly His Ala Ala Glu Cys Asn Val His Gly Val Cys He Ala Cys 745 750 755 760 Ala His Asn Thr Thr Gly Val His Cys Glu Gin Cys Leu Pro Gly Phe Tyr Gly Glu Pro 765 770 775 780 Ser Arg Gly Thr Pro Gly Asp Cys Gin Pro Cys Ala Cys Pro Leu Thr He Ala Ser Asn 785 790 795 800 Asn Phe Ser Pro Thr Cys His Leu Asn Asp Gly Asp Glu Val Val Cys Asp Trp Cys Ala 805 810 815 820 Pro Gly Tyr Ser Gly Ala Trp Cys Glu Arg Cys Ala Asp Gly Tyr Tyr Gly Asn Pro Thr 825 830 835 840 Val Pro Gly Glu Ser Cys Val Pro Cys Asp Cys Ser Gly Asn Val Asp Pro Ser Glu Ala 845 850 855 860 Gly His Cys Asp Ser Val Thr Gly Glu Cys Leu Lys Cys Leu Gly Asn Thr Asp Gly Ala 865 870 875 880 His Cys Glu Arg Cys Ala Asp Gly Phe Tyr Gly Asp Ala Val Thr Ala Lys Asn Cys Arg 885 890 895 900 Ala Cys Glu Cys His Val Lys Gly Ser His Ser Ala Val Cys His Leu Glu Thr Gly Leu 905 910 915 920 Cys Asp Cys Lys Pro Asn Val Thr Gly Gin Gin Cys Asp Gin Cys Leu His Gly Tyr Tyr 925 930 935 940 Gly Leu Asp Ser Gly His Gly Cys Arg Pro Cys Asn Cys ser Val Ala Gly Ser Val Ser 945 950 955 960 Asp Gly Cys Thr Asp Glu Gly Gin Cys His Cys Val Pro Gly Val Ala Gly Lys Arg Cys 965 970 975 980 Asp Arg Cys Ala His Gly Phe Tyr Ala Tyr Gin Asp Gly Ser Cys Thr Pro Cys Asp Cys 985 990 995 1000 Pro His Thr Gin Asn Thr Cys Asp Pro Glu Thr Gly Glu Cys Val Cys Pro Pro His Thr 1005 1010 1015 1020 Gin Gly Gly Lys Cys Glu Glu Cys Glu Asp Gly His Trp Gly Tyr Asp Ala Glu Val Gly 1025 1030 1035 1040 Cys Gin Ala Cys Asn Cys Ser Leu Val Gly Ser Thr His His Arg Cys Asp Val Val Thr 1045 1050 1055 1060 Gly His Cys Gin Cys Lys Ser Lys Phe Gly Gly Arg Ala Cys Asp Gin Cys Ser Leu Gly 1065 1070 1075 1080 Tyr Arg Asp Phe Pro Asp Cys Val Pro Cys Asp Cys Asp Leu Arg Gly Thr Ser Gly Asp 1085 1090 1095 1100 Ala Cys Asn Leu Glu Gin Gly Leu Cys Gly Cys Val Glu Glu Thr Gly Ala Cys Pro Cys 1105 1110 1115 1120 Lys Glu Asn Val Phe Gly Pro Gin Cys Asn Glu Cys Arg Glu Gly Thr Phe Ala Leu Arg 1125 1130 1135 1140 Ala Asp Asn Pro Leu Gly Cys Ser Pro Cys Phe Cys Ser Gly Leu Ser His Leu Cys Ser 1145 1150 1155 1160 Glu Leu Glu Asp Tyr Val Arg Thr Pro Val Thr Leu Gly Ser Asp Gin Pro Leu Leu Arg 1165 1170 1175 1180 Val Val Ser Gin Ser Asn Leu Arg Gly Thr Thr Glu Gly Val Tyr Tyr Gin Ala Pro Asp 1185 1190 1195 1200 Phe Leu Leu Asp Ala Ala Thr Val Arg Gin His He Arg Ala Glu Pro Phe Tyr Trp Arg 1205 1210 1215 1220 Leu Pro Gin Gin Phe Gin Gly Asp Gin Leu Met Ala Tyr Gly Gly Lys Leu Lys Tyr Ser 1225 1230 1235 1240 Val Ala Phe Tyr Ser Leu Asp Gly Val Gly Thr Ser Asn Phe Glu Pro Gin Val Leu He 1245 1250 1255 1260 Lys Gly Gly Arg He Arg Lys Gin Val He Tyr Met Asp Ala Pro Ala Pro Glu Asn Gly 1265 1270 1275 1280 Val Arg Gin Glu Gin Glu Val Ala Met Arg Glu Asn Phe Trp Lys Tyr Phe Asn Ser Val 1285 1290 1295 1300 Ser Glu Lys Pro Val Thr Arg Glu Asp Phe Met Ser Val Leu Ser Asp He Glu Tyr He 1305 1310 1315 1320 Leu He Lys Ala Ser Tyr Gly Gin Gly Leu Gin Gin Ser Arg He Ser Asp He Ser Val 1325 1330 1335 1340 Glu Val Gly Arg Lys Ala Glu Lys Leu His Pro Glu Glu Glu Val Ala Ser Leu Leu Glu 1345 1350 1355 1360 Asn Cys Val Cys Pro Pro Gly Thr Val Gly Phe Ser Cys Gin Asp Cys Ala Pro Gly Tyr 1365 1370 1375 1380 His Arg Gly Lys Leu Pro Ala Gly Ser Asp Arg Gly Pro Arg Pro Leu Val Ala Pro Cys 1385 1390 1395 1400 Val Pro Cys Ser Cys Asn Asn His Ser Asp Thr Cys Asp Pro Asn Thr Gly Lys Cys Leu 1405 1410 1415 1420 Asn Cys Gly Asp Asn Thr Ala Jly Asp His Cys Asp Val Cys Thr Ser Gly Tyr Tyr Gly 1425 1430 1435 1440 Lys Val Thr Gly Ser Ala Ser Asp Cys Ala Leu Cys Ala Cys Pro His Ser Pro Pro Ala 1445 1450 1455 1460 Ser Phe Ser Pro Thr Cys Val Leu Glu Gly Asp His Asp Phe Arg Cys Asp Ala Cys Leu 1465 1470 1475 1480 Leu Gly Tyr Glu Gly Lys His Cys Glu Arg Cys Ser Ser Ser Tyr Tyr Gly Asn Pro Gin 1485 1490 1495 1500 Thr Pro Gly Gly Ser Cys Gin Lys Cys Asp Cys Asn Arg His Gly Ser Val His Gly Asp 1505 1510 1515 1520 Cys Asp Arg Thr Ser Gly Gin Cys Val Cys Arg Leu Gly Ala Ser Gly Leu Arg Cys Asp 1525 1530 1535 1540 Glu Cys Glu Pro Arg His He Leu Met Glu Thr Asp Cys Val Ser Cys Asp Asp Glu Cys 1545 1550 1555 1560 Val Gly Val Leu Leu Asn Asp Leu Asp Glu He Gly Asp Ala Val Leu Ser Leu Asn Leu 1565 1570 1575 1580 Thr Gly He He Pro Val Pro Tyr Gly He Leu Ser Asn Leu Glu Asn Thr Thr Lys Tyr 1585 1590 1595 1600 Leu Gin Glu Ser Leu Leu Lys Glu Asn Met Gin Lys Asp Leu Gly Lys He Lys Leu Glu 1605 1610 1615 1620 Gly Val Ala Glu Glu Thr Asp Asn Leu Gin Lys Lys Leu Thr Arg Met Leu Ala Ser Thr 1625 1630 1635 1640 Gin Lys Val Asn Arg Ala Thr Glu Arg He Phe Lys Glu Ser Gin Asp Leu Ala Val Ala 1645 1650 1655 1660 He Glu Arg Leu Gin Met Ser He Thr Glu He Met Glu Lys Thr Thr Leu Asn Gin Thr 1665 1670 1675 1680 Leu Asp Glu Asp Phe Leu Leu Pro Asn Ser Thr Leu Gin Asn Met Gin Gin Asn Gly Thr 1685 1690 1695 1700 Ser Leu Leu Glu He Met Gin He Arg Asp Phe Thr Gin Leu His Gin Asn Ala Thr Leu 1705 1710 1715 1720 Glu Leu Lys Ala Ala Glu Asp Leu Leu Ser Gin He Gin Glu Asn Tyr Gin Lys Pro Leu 1725 1730 1735 1740 Glu Glu Leu Glu Val Leu Lys Glu Ala Ala Ser His Val Leu Ser Lys His Asn Asn Glu 1745 1750 1755 1760 Leu Lys Ala Ala Glu Ala Leu Val Arg Glu Ala Glu Ala Lys Met Gin Glu Ser Asn His 1765 1770 1775 1780 Leu Leu Leu Met Val Asn Ala Asn Leu Arg Glu Phe Ser Asp Lys Lys Leu His Val Gin 1785 1790 1795 1800 Glu Glu Gin Asn Leu Thr Ser Glu Leu He Val Gin Gly Arg Gly Leu He Asp Ala Ala 1805 1810 1815 1820 Ala Ala Gin Thr Asp Ala Val Gin Asp Ala Leu Glu His Leu Glu Asp His Gin Asp Lys 1825 1830 1835 1840 Leu Leu Leu Trp Ser Ala Lys He Arg His His He Asp Asp Leu Val Met His Met Ser 1845 1850 1855 1860 Gin Arg Asn Ala Val Asp Leu Val Tyr Arg Ala Glu Asp His Ala Thr Glu Phe Gin Arg 1865 1870 1875 1880 Leu Ala Asp Val Leu Tyr Ser Gly Leu Glu Asn He Arg Asn Val Ser Leu Asn Ala Thr 1885 1890 1895 1900 Ser Ala Ala Tyr Val His Tyr Asn He Gin Ser Leu He Glu Glu Ser Glu Glu Leu Ala 1905 1910 1915 1920 Arg Asp Ala His Arg Thr Val Thr Glu Thr Ser Leu Leu Ser Glu Ser Leu Val Ser Asn 1925 1930 1935 1940 Gly Lys Ala Ala Val Gin Arg Ser Ser Arg Phe Leu Lys Glu Gly Asn Asn Leu Ser Arg 1945 1950 1955 1960 Lys Leu Pro Gly He Ala Leu Glu Leu Ser Glu Leu Arg Asn Lys Thr Asn Arg Phe Gin 1965 1970 1975 1980 Glu Asn Ala Val Glu He Thr Arg Gin Thr Asn Glu Ser Leu Leu He Leu Arg Ala He 1985 1990 1995 2000 Pro Glu Gly He Arg Asp Lys Gly Ala Lys Thr Lys Glu Leu Ala Thr Ser Ala Ser Gin 2005 2010 2015 2020 Ser Ala Val Ser Thr Leu Arg Asp Val Ala Gly Leu Ser Gin Glu Leu Leu Asn Thr Ser 2025 2030 2035 2040 Ala Ser Leu Ser Arg Val Asn Thr Thr Leu Arg Glu Thr His Gin Leu Leu Gin Asp Ser 2045 2050 2055 2060 Thr Met Ala Thr Leu Leu Ala Gly Arg Lys Val Lys Asp Val Glu He Gin Ala Asn Leu 2065 2070 2075 2080 Leu Phe Asp Arg Leu Lys Pro Leu Lys Met Leu Glu Glu Asn Leu Ser Arg Asn Leu Ser 2085 2090 2095 2100 Glu He Lys Leu Leu He Ser Gin Ala Arg Lys Gin Ala Ala Ser He Lys Val Ala Val 2105 2110 2115 2120 Ser Ala Asp Arg Asp Cys He Arg Ala Tyr Gin Pro Gin He Ser Ser Thr Asn Tyr Asn 2125 2130 2135 2140 Thr Leu Thr Leu Asn Val Lys Thr Gin Glu Pro Asp Asn Leu Leu Phe Tyr Leu Gly Ser 2145 2150 2155 2160 Ser Thr Ala Ser Asp Phe Leu Ala Val Glu Met Arg Arg Gly Arg Val Ala Phe Leu Trp 2165 2170 2175 2180 Asp Leu Gly Ser Gly Ser Thr Arg Leu Glu Phe Pro Asp Phe Pro He Asp Asp Asn Arg 2185 2190 2195 2200 Trp His Ser He His Val Ala Arg Phe Gly Asn He Gly Ser Leu Ser Val Lys Glu Met 2205 2210 2215 2220 Ser Ser Asn Gin Lys Ser Pro Thr Lys Thr Ser Lys Ser Pro Gly Thr Ala Asn Val Leu 2225 2230 2235 2240 Asp Val Asn Asn Ser Thr Leu Met Phe Val Gly Gly Leu Gly Gly Gin He Lys Lys Ser 2245 2250 2255 2260 Pro Ala Val Lys Val Thr His Phe Lys Gly Cys Leu Gly Glu Ala Phe Leu Asn Gly Lys 2265 2270 2275 2280 Ser He Gly Leu Trp Asn Tyr He Glu Arg Glu Gly Lys Cys Arg Gly Cys Phe Gly Ser 2285 2290 2295 2300 Ser Gin Asn Glu Asp Pro Ser Phe His Phe Asp Gly Ser Gly Tyr Ser Val Val Glu Lys 2305 2310 2315 2320 Ser Leu Pro Ala Thr Val Thr Gin He He Met Leu Phe Asn Thr Phe Ser Pro Asn Gly 2325 2330 2335 2340 Leu Leu Leu Tyr Leu Gly Ser Tyr Gly Thr Lys Asp Phe Leu Ser He Glu Leu Phe Arg 2345 2350 2355 2360 Gly Arg Val Lys Val Met Thr Asp Leu Gly Ser Gly Pro He Thr Leu Leu Thr Asp Arg 2365 2370 2375 2380 Arg Tyr Asn Asn Gly Thr Trp Tyr Lys He Ala Phe Gin Arg Asn Arg Lys Gin Gly Val 2385 2390 2395 2400 Leu Ala Val He Asp Ala Tyr Asn Thr Ser Asn Lys Glu Thr Lys Gin Gly Glu Thr Pro 2405 2410 2415 2420 Gly Ala Ser Ser Asp Leu Asn Arg Leu Asp Lys Asp Pro He Tyr Val Gly Gly Leu Pro 2425 2430 2435 2440 Arg Ser Arg Val Val Arg Arg Gly Val Thr Thr Lys Ser Phe Val Gly Cys He Lys Asn 2445 2450 2455 2460 Leu Glu He Ser Arg Ser Thr Phe Asp Leu Leu Arg Asn Ser Tyr Gly Val Arg Lys Gly 2465 2470 2475 2480 Cys Leu Leu Glu Pro He Arg Ser Val Ser Phe Leu Lys Gly Gly Tyr He Glu Leu Pro 2485 2490 2495 2500 Pro Lys Ser Leu Ser Pro Glu Ser Glu Trp Leu Val Thr Phe Ala Thr Thr Asn Ser Ser 2505 2510 2515 2520 Gly He He Leu Ala Ala Leu Gly Gly Asp Val Glu Lys Arg Gly Asp Arg Glu Glu Ala 2525 2530 2535 2540 His Val Pro Phe Phe Ser Val Met Leu He Gly Gly Asn He Glu Val His Val Asn Pro 2545 2550 2555 2560 Gly Asp Gly Thr Gly Leu Arg Lys Ala Leu Leu His Ala Pro Thr Gly Thr Cys Ser Asp 2565 2570 2575 2580 Gly Gin Ala His Ser He Ser Leu Val Arg Asn Arg Arg He He Thr Val Gin Leu Asp 2585 2590 2595 2600 Glu Asn Asn Pro Val Glu Met Lys Leu Gly Thr Leu Val Glu Ser Arg Thr He Asn Val 2605 2610 2615 2620 Ser Asn Leu Tyr Val Gly Gly He Pro Glu Gly Glu Gly Thr Ser Leu Leu Thr Met Arg 2625 2630 2635 2640 Arg Ser Phe His Gly Cys He Lys Asn Leu He Phe Asn Leu Glu Leu Leu Asp Phe Asn 2645 2650 2655 2660 Ser Ala Val Gly His Glu Gin Val Asp Leu Asp Thr Cys Trp Leu Ser Glu Arg Pro Lys 2665 2670 2675 2680 Leu Ala Pro Asp Ala Glu Asp Ser Lys Leu Leu Arg Glu Pro Arg Ala Phe Pro Glu Gin 2685 2690 2695 2700 Cys Val Val Asp Ala Ala Leu Glu Tyr Val Pro Gly Ala His Gin Phe Gly Leu Thr Gin 2705 2710 2715 2720 Asn Ser His Phe He Leu Pro Phe Asn Gin Ser Ala Val Arg Lys Lys Leu Ser Val Glu 2725 2730 2735 2740 Leu Ser He Arg Thr Phe Ala Ser Ser Gly Leu He Tyr Tyr Met Ala His Gin Asn Gin 2745 2750 2755 2760 Ala Asp Tyr Ala Val Leu Gin Leu His Gly Gly Arg Leu His Phe Met Phe Asp Leu Gly 2765 2770 2775 2780 Lys Gly Arg Thr Lys Val Ser His Pro Ala Leu Leu Ser Asp Gly Lys Trp His Thr Val 2785 2790 2795 2800 Lys Thr Asp Tyr Val Lys Arg Lys Gly Phe He Thr Val Asp Gly Arg Glu Ser Pro Met 2805 2810 2815 2820 Val Thr Val Val Gly Asp Gly Thr Met Leu Asp Val Glu Gly Leu Phe Tyr Leu Gly Gly 2825 2830 2835 2840 Leu Pro Ser Gin Tyr Gin Ala Arg Lys He Gly Asn He Thr His Ser He Pro Ala Cys 2845 2850 2855 2860 He Gly Asp Val Thr Val Asn Ser Lys Gin Leu Asp Lys Asp Ser Pro Val Ser Ala Phe 2865 2870 2875 2880 Thr Val Asn Arg Cys Tyr Ala Val Ala Gin Glu Gly Thr Tyr Phe Asp Gly Ser Gly Tyr 2885 2890 2895 2900 Ala Ala Leu Val Lys Glu Gly Tyr Lys Val Gin Ser Asp Val Asn He Thr Leu Glu Phe 2905 2910 2915 2920 Arg Thr Ser Ser Gin Asn Gly Val Leu Leu Gly He Ser Thr Ala Lys Val Asp Ala He 2925 2930 2935 2940 Gly Leu Glu Leu Val Asp Gly Lys Val Leu Phe His Val Asn Asn Gly Ala Gly Arg He 2945 2950 2955 2960 Thr Pro Ala Tyr Glu Pro Lys Thr Ala Thr Val Leu Cys Asp Gly Lys Trp His Thr Leu 2965 2970 2975 2980 Gin Ala Asn Lys Ser Lys His Arg He Thr Leu He Val Asp Gly Asn Ala Val Gly Ala 2985 2990 2995 3000 Glu Ser Pro His Thr Gin Ser Thr Ser Val Asp Thr Asn Asn Pro He Tyr Val Gly Gly 3005 3010 3015 3020 Tyr Pro Ala Gly Val Lys Gin Lys Cys Leu Arg Ser Gin Thr Ser Phe Arg Gly Cys Leu 3025 3030 3035 3040 Arg Lys Leu Ala Leu He Lys Ser Pro Gin Val Gin Ser Phe Asp Phe Ser Arg Ala Phe 3045 3050 3055 3060 Glu Leu His Gly Val Phe Leu His Ser Cys Pro Gly Thr Glu Ser 3065 3070 3075 INFORMATION FOR SEQ ID NO: G: SEQUENCE CHARACTERISTICS (A) LENGTH: 1786 AMINO ACIDS (B) TYPE: AMINO ACID (C) STRANDEDNESS: (D) TOPOLOGY: LINEAR (E) AMINO ACID NUMBERING ACCORDING TO TRANSLATION OF GENEBANK ACCESSION NUMBER P07942; MOLECULAR TYPE: PROTEIN SEQUENCE DESCRIPTION: SEQ ID NO 6: Met Gly Leu Leu Gin Leu Leu Ala Phe Ser Phe Leu Ala Leu Cys Arg Ala Arg Val Arg 1 5 10 15 20 Ala Gin Glu Pro Glu Phe Ser Tyr Gly Cys Ala Glu Gly Ser Cys Tyr Pro Ala Thr Gly 25 30 35 40 Asp Leu Leu He Gly Arg Ala Gin Lys Leu Ser Val Thr Ser Thr Cys Gly Leu His Lys 45 50 55 60 Pro Glu Pro Tyr Cys He Val Ser His Leu Gin Glu Asp Lys Lys Cys Phe He Cys Asn 65 70 75 80 Ser Gin Asp Pro Tyr His Glu Thr Leu Asn Pro Asp Ser His Leu He Glu Asn Val Val 85 90 95 100 Thr Thr Phe Ala Pro Asn Arg Leu Lys He Trp Trp Gin Ser Glu Asn Gly Val Glu Asn 105 110 115 120 Val Thr He Gin Leu Asp Leu Glu Ala Glu Phe His Phe Thr His Leu He Met Thr Phe 125 130 135 140 Lys Thr Phe Arg Pro Ala Ala Met Leu He Glu Arg Ser Ser Asp Phe Gly Lys Thr Trp 145 150 155 160 Gly Val Tyr Arg Tyr Phe Ala Tyr Asp Cys Glu Ala Ser Phe Pro Gly He Ser Thr Gly 165 170 175 180 Pro Met Lys Lys Val Asp Asp He He Cys Asp Ser Arg Tyr Ser Asp He Glu Pro Ser 185 190 195 200 Thr Glu Gly Glu Val He Phe Arg Ala Leu Asp Pro Ala Phe Lys He Glu Asp Pro Tyr 205 210 215 220 Ser Pro Arg He Gin Asn Leu Leu Lys He Thr Asn Leu Arg He Lys Phe Val Lys Leu 225 230 235 240 His Thr Leu Gly Asp Asn Leu Leu Asp Ser Arg Met Glu He Arg Glu Lys Tyr Tyr Tyr 245 250 255 260 Ala Val Tyr Asp Met Val Val Arg Gly Asn Cys Phe Cys Tyr Gly His Ala Ser Glu Cys 265 270 275 280 Ala Pro Val Asp Gly Phe Asn Glu Glu Val Glu Gly Met Val His Gly His Cys Met Cys 285 290 295 300 Arg His Asn Thr Lys Gly Leu Asn Cys Glu Leu Cys Met Asp Phe Tyr His Asp Leu Pro 305 310 315 320 Trp Arg Pro Ala Glu Gly Arg Asn Ser Asn Ala Cys Lys Lys Cys Asn Cys Asn Glu His 325 330 335 340 Ser He Ser Cys His Phe Asp Met Ala Val Tyr Leu Ala Thr Gly Asn Val Ser Gly Gly 345 350 355 360 Val Cys Asp Asp Cys Gin His Asn Thr Met Gly Arg Asn Cys Glu Gin Cys Lys Pro Phe 365 370 375 380 Tyr Tyr Gin His Pro Glu Arg Asp He Arg Asp Pro Asn Phe Cys Glu Arg Cys Thr Cys 385 390 395 400 Asp Pro Ala Gly Ser Gin Asn Glu Gly He Cys Asp Ser Tyr Thr Asp Phe Ser Thr Gly 405 410 415 420 Leu He Ala Gly Gin Cys Arg Cys Lys Leu Asn Val Glu Gly Glu His Cys Asp Val Cys 425 430 435 440 Lys Glu Gly Phe Tyr Asp Leu Ser Ser Glu Asp Pro Phe Gly Cys Lys Ser Cys Ala Cys 445 450 455 460 Asn Pro Leu Gly Thr He Pro Gly Gly Asn Pro Cys Asp Ser Glu Thr Gly His Cys Tyr 465 470 475 480 Cys Lys Arg Leu Val Thr Gly Gin His Cys Asp Gin Cys Leu Pro Glu His Trp Gly Leu 485 490 495 500 Ser Asn Asp Leu Asp Gly Cys Arg Pro Cys Asp Cys Asp Leu Gly Gly Ala Leu Asn Asn 505 510 515 520 Ser Cys Phe Ala Glu Ser Gly Gin Cys Ser Cys Arg Pro His Met He Gly Arg Gin Cys 525 530 535 540 Asn Glu Val Glu Pro Gly Tyr Tyr Phe Ala Thr Leu Asp His Tyr Leu Tyr Glu Ala Glu 545 550 555 560 Glu Ala Asn Leu Gly Pro Gly Val Ser He Val Glu Arg Gin Tyr He Gin Asp Arg He 565 570 575 580 Pro Ser Trp Thr Gly Ala Gly Phe Val Arg Val Pro Glu Gly Ala Tyr Leu Glu Phe Phe 585 590 595 600 He Asp Asn He Pro Tyr Ser Met Glu Tyr Asp He Leu He Arg Tyr Glu Pro Gin Leu 605 610 615 620 Pro Asp His Trp Glu Lys Ala Val He Thr Val Gin Arg Pro Gly Arg He Pro Thr Ser 625 630 635 640 Ser Arg Cys Gly Asn Thr He Pro Asp Asp Asp Asn Gin Val Val Ser Leu Ser Pro Gly 645 650 655 660 Ser Arg Tyr Val Val Leu Pro Arg Pro Val Cys Phe Glu Lys Gly Thr Asn Tyr Thr Val 665 670 675 680 Arg Leu Glu Leu Pro Gin Tyr Thr Ser Ser Asp Ser Asp Val Glu Ser Pro Tyr Thr Leu 685 690 695 700 He Asp Ser Leu Val Leu Met Pro Tyr Cys Lys Ser Leu Asp He Phe Thr Val Gly Gly 705 710 715 720 Ser Gly Asp Gly Val Val Thr Asn Ser Ala Trp Glu Thr Phe Gin Arg Tyr Arg Cys Leu 725 730 735 740 Glu Asn Ser Arg Ser Val Val Lys Thr Pro Met Thr Asp Val Cys Arg Asn He He Phe 745 750 755 760 Ser He Ser Ala Leu Leu His Gin Thr Gly Leu Ala Cys Glu Cys Asp Pro Gin Gly Ser 765 770 775 780 Leu Ser Ser Val Cys Asp Pro Asn Gly Gly Gin Cys Gin Cys Arg Pro Asn Val Val Gly 785 790 795 800 Arg Thr Cys Asn Arg Cys Ala Pro Gly Thr Phe Gly Phe Gly Pro Ser Gly Cys Lys Pro 805 810 815 820 Cys Glu Cys His Leu Gin Gly Ser Val Asn Ala Phe Cys Asn Pro Val Thr Gly Gin Cys 825 830 835 840 His Cys Phe Gin Gly Val Tyr Ala Arg Gin Cys Asp Arg Cys Leu Pro Gly His Trp Gly 845 850 855 860 Phe Pro Ser Cys Gin Pro Cys Gin Cys Asn Gly His Ala Asp Asp Cys Asp Pro Val Thr 865 870 875 880 Gly Glu Cys Leu Asn Cys Gin Asp Tyr Thr Met Gly His Asn Cys Glu Arg Cys Leu Ala 885 890 895 900 Gly Tyr Tyr Gly Asp Pro He He Gly Ser Gly Asp His Cys Arg Pro Cys Pro Cys Pro 905 910 915 920 Asp Gly Pro Asp Ser Gly Arg Gin Phe Ala Arg Ser Cys Tyr Gin Asp Pro Val Thr Leu 925 930 935 940 Gin Leu Ala Cys Val Cys Asp Pro Gly Tyr He Gly Ser Arg Cys Asp Asp Cys Ala Ser 945 950 955 960 Gly Tyr Phe Gly Asn Pro Ser Glu Val Gly Gly Ser Cys Gin Pro Cys Gin Cys His Asn 965 970 975 980 Asn He Asp Thr Thr Asp Pro Glu Ala Cys Asp Lys Glu Thr Gly Arg Cys Leu Lys Cys 985 990 995 1000 Leu Tyr His Thr Glu Gly Glu His Cys Gin Phe Cys Arg Phe Gly Tyr Tyr Gly Asp Ala 1005 1010 1015 1020 Leu Arg Gin Asp Cys Arg Lys Cys Val Cys Asn Tyr Leu Gly Thr Val Gin Glu His Cys 1025 1030 1035 1040 Asn Gly Ser Asp Cys Gin Cys Asp Lys Ala Thr Gly Gin Cys Leu Cys Leu Pro Asn Val 1045 1050 1055 1060 He Gly Gin Asn Cys Asp Arg Cys Ala Pro Asn Thr Trp Gin Leu Ala Ser Gly Thr Gly 1065 1070 1075 1080 Cys Asp Pro Cys Asn Cys Asn Ala Ala His Ser Phe Gly Pro Ser Cys Asn Glu Phe Thr 1085 1090 1095 1100 Gly Gin Cys Gin Cys Met Pro Gly Phe Gly Gly Arg Thr Cys Ser Glu Cys Gin Glu Leu 1105 1110 1115 1120 Phe Trp Gly Asp Pro Asp Val Glu Cys Arg Ala Cys Asp Cys Asp Pro Arg Gly He Glu 1125 1130 1135 1140 Thr Pro Gin Cys Asp Gin Ser Thr Gly Gin Cys Val Cys Val Glu Gly Val Glu Gly Pro 1145 1150 1155 1160 Arg Cys Asp Lys Cys Thr Arg Gly Tyr Ser Gly Val Phe Pro Asp Cys Thr Pro Cys His 1165 1170 1175 1180 Gin Cys Phe Ala Leu Trp Asp Val He He Ala Glu Leu Thr Asn Arg Thr His Arg Phe 1185 1190 1195 1200 Leu Glu Lys Ala Lys Ala Leu Lys He Ser Gly Val He Gly Pro Tyr Arg Glu Thr Val 1205 1210 1215 1220 Asp Ser Val Glu Arg Lys Val Ser Glu He Lys Asp He Leu Ala Gin Ser Pro Ala Ala 1225 1230 1235 1240 Glu Pro Leu Lys Asn He Gly Asn Leu Phe Glu Glu Ala Glu Lys Leu He Lys Asp Val 1245 1250 1255 1260 Thr Glu Met Met Ala Gin Val Glu Val Lys Leu Ser Asp Thr Thr Ser Gin Ser Asn Ser 1265 1270 1275 1280 Thr Ala Lys Glu Leu Asp Ser Leu Gin Thr Glu Ala Glu Ser Leu Asp Asn Thr Val Lys 1285 1290 1295 1300 Glu Leu Ala Glu Gin Leu Glu Phe He Lys Asn Ser Asp He Arg Gly Ala Leu Asp Ser 1305 1310 1315 1320 He Thr Lys Tyr Phe Gin Met Ser Leu Glu Ala Glu Glu Arg Val Asn Ala Ser Thr Thr 1325 1330 1335 1340 Glu Pro Asn Ser Thr Val Glu Gin Ser Ala Leu Met Arg Asp Arg Val Glu Asp Val Met 1345 1350 1355 1360 Met Glu Arg Glu Ser Gin Phe Lys Glu Lys Gin Glu Glu Gin Ala Arg Leu Leu Asp Glu 1365 1370 1375 1380 Leu Ala Gly Lys Leu Gin Ser Leu Asp Leu Ser Ala Ala Ala Glu Met Thr Cys Gly Thr 1385 1390 1395 1400 Pro Pro Gly Ala Ser Cys Ser Glu Thr Glu Cys Gly Gly Pro Asn Cys Arg Thr Asp Glu 1405 1410 1415 1420 Gly Glu Arg Lys Cys Gly Gly Pro Gly Cys Gly Gly Leu Val Thr Val Ala His Asn Ala 1425 1430 1435 1440 Trp Gin Lys Ala Met Asp Leu Asp Gin Asp Val Leu Ser Ala Leu Ala Glu Val Glu Gin 1445 1450 1455 1460 Leu Ser Lys Met Val Ser Glu Ala Lys Leu Arg Ala Asp Glu Ala Lys Gin Ser Ala Glu 1465 1470 1475 1480 Asp He Leu Leu Lys Thr Asn Ala Thr Lys Glu Lys Met Asp Lys Ser Asn Glu Glu Leu 1485 1490 1495 1500 Arg Asn Leu He Lys Gin He Arg Asn Phe Leu Thr Gin Asp Ser Ala Asp Leu Asp Ser 1505 1510 1515 1520 He Glu Ala Val Ala Asn Glu Val Leu Lys Met Glu Met Pro Ser Thr Pro Gin Gin Leu 1525 1530 1535 1540 Gin Asn Leu Thr Glu Asp He Arg Glu Arg Val Glu Ser Leu Ser Gin Val Glu Val He 1545 1550 1555 1560 Leu Gin His Ser Ala Ala Asp He Ala Arg Ala Glu Met Leu Leu Glu Glu Ala Lys Arg 1565 1570 1575 1580 Ala Ser Lys Ser Ala Thr Asp Val Lys Val Thr Ala Asp Met Val Lys Glu Ala Leu Glu 1585 1590 1595 1600 Glu Ala Glu Lys Ala Gin Val Ala Ala Glu Lys Ala He Lys Gin Ala Asp Glu Asp He 1605 1610 1615 1620 Gin Gly Thr Gin Asn Leu Leu Thr Ser He Glu Ser Glu Thr Ala Ala Ser Glu Glu Thr 1625 1630 1635 1640 Leu Phe Asn Ala Ser Gin Arg He Ser Glu Leu Glu Arg Asn Val Glu Glu Leu Lys Arg 1645 1650 1655 1660 Lys Ala Ala Gin Asn Ser Gly Glu Ala Glu Tyr He Glu Lys Val Val Tyr Thr Val Lys 1665 1670 1675 1680 Gin Ser Ala Glu Asp Val Lys Lys Thr Leu Asp Gly Glu Leu Asp Glu Lys Tyr Lys Lys 1685 1690 1695 1700 Val Glu Asn Leu He Ala Lys Lys Thr Glu Glu Ser Ala Asp Ala Arg Arg Lys Ala Glu 1705 1710 1715 1720 Met Leu Gin Asn Glu Ala Lys Thr Leu Leu Ala Gin Ala Asn Ser Lys Leu Gin Leu Leu 1725 1730 1735 1740 Lys Asp Leu Glu Arg Lys Tyr Glu Asp Asn Gin Arg Tyr Leu Glu Asp Lys Ala Gin Glu 1745 1750 1755 1760 Leu Ala Arg Leu Glu Gly Glu Val Arg Ser Leu Leu Lys Asp He Ser Gin Lys Val Ala 1765 1770 1775 1780 Val Tyr Ser Thr Cys Leu 1785 INFORMATION FOR SEQ ID NO: 7: SEQUENCE CHARACTERISTICS (A) LENGTH: 1786 AMINO ACIDS (B) TYPE: AMINO ACID (C) STRANDEDNESS: (D) TOPOLOGY: LINEAR (E) AMINO ACID NUMBERING ACCORDING TO TRANSLATION OF GENEBANK ACCESSION NUMBER P02469; MOLECULAR TYPE: PROTEIN SEQUENCE DESCRIPTION: SEQ ID NO 7: Met Gly Leu Leu Gin Val Phe Ala Phe Gly Val Leu Ala Leu Trp Gly Thr Arg Val Cys 1 5 10 15 20 Ala Gin Glu Pro Glu Phe Ser Tyr Gly Cys Ala Glu Gly Ser Cys Tyr Pro Ala Thr Gly 25 30 35 40 Asp Leu Leu He Gly Arg Ala Gin Lys Leu Ser Val Thr Ser Thr Cys Gly Leu His Lys 45 50 55 60 Pro Glu Pro Tyr Cys He Val Ser His Leu Gin Glu Asp Lys Lys Cys Phe He Cys Asp 65 70 75 80 Ser Arg Asp Pro Tyr His Glu Thr Leu Asn Pro Asp Ser His Leu He Glu Asn Val Val 85 90 95 100 Thr Thr Phe Ala Pro Asn Arg Leu Lys He Trp Trp Gin Ser Glu Asn Gly Val Glu Asn 105 110 115 120 Val Thr He Gin Leu Asp Leu Glu Ala Glu Phe His Phe Thr His Leu He Met Thr Phe 125 130 135 140 Lys Thr Phe Arg Pro Ala Ala Met Leu He Glu Arg Ser Ser Asp Phe Gly Lys Thr Trp 145 150 155 160 Gly Val Tyr Arg Tyr Phe Ala Tyr Asp Cys Glu Ser Ser Phe Pro Gly He Ser Thr Gly 165 170 175 180 Pro Met Lys Lys Val Asp Asp He He Cys Asp Ser Arg Tyr Ser Asp He Glu Pro Ser 185 190 195 200 Thr Glu Gly Glu Val He Phe Arg Ala Leu Asp Pro Ala Phe Lys He Glu Asp Pro Tyr 205 210 215 220 Ser Pro Arg He Gin Asn Leu Leu Lys He Thr Asn Leu Arg He Lys Phe Val Lys Leu 225 230 235 240 His Thr Leu Gly Asp Asn Leu Leu Asp Ser Arg Met Glu He Arg Glu Lys Tyr Tyr Tyr 245 250 255 260 Ala Val Tyr Asp Met Val Val Arg Gly Asn Cys Phe Cys Tyr Gly His Ala Ser Glu Cys 265 270 275 280 Ala Pro Val Asp Gly Val Asn Glu Glu Val Glu Gly Met Val His Gly His Cys Met Cys 285 290 295 300 Arg His Asn Thr Lys Gly Leu Asn Cys Glu Leu Cys Met Asp Phe Tyr His Asp Leu Pro 305 310 315 320 Trp Arg Pro Ala Glu Gly Arg Asn Ser Asn Ala Cys Lys Lys Cys Asn Cys Asn Glu His 325 330 335 340 Ser Ser Ser Cys His Phe Asp Met Ala Val Phe Leu Ala Thr Gly Asn Val Ser Gly Gly 345 350 355 360 Val Cys Asp Asn Cys Gin His Asn Thr Met Gly Arg Asn Cys Glu Gin Cys Lys Pro Phe 365 370 375 380 Tyr Phe Gin His Pro Glu Arg Asp He Arg Asp Pro Asn Leu Cys Glu Pro Cys Thr Cys 385 390 395 400 Asp Pro Ala Gly Ser Glu Asn Gly Gly He Cys Asp Gly Tyr Thr Asp Phe Ser Val Gly 405 410 415 420 Leu He Ala Gly Gin Cys Arg Cys Lys Leu His Val Glu Gly Glu Arg Cys Asp Val Cys 425 430 435 440 Lys Glu Gly Phe Tyr Asp Leu Ser Ala Glu Asp Pro Tyr Gly Cys Lys Ser Cys Ala Cys 445 450 455 460 Asn Pro Leu Gly Thr He Pro Gly Gly Asn Pro Cys Asp Ser Glu Thr Gly Tyr Cys Tyr 465 470 475 480 Cys Lys Arg Leu Val Thr Gly Gin Arg Cys Asp Gin Cys Leu Pro Gin His Trp Gly Leu 485 490 495 500 Ser Asn Asp Leu Asp Gly Cys Arg Pro Cys Asp Cys Asp Leu Gly Gly Ala Leu Asn Asn 505 510 515 520 Ser Cys Ser Glu Asp Ser Gly Gin Cys Ser Cys Leu Pro His Met He Gly Arg Gin Cys 525 530 535 540 Asn Glu Val Glu Ser Gly Tyr Tyr Phe Thr Thr Leu Asp His Tyr He Tyr Glu Ala Glu 545 550 555 560 Glu Ala Asn Leu Gly Pro Gly Val Val Val Val Glu Arg Gin Tyr He Gin Asp Arg He 565 570 575 580 Pro Ser Trp Thr Gly Pro Gly Phe Val Arg Val Pro Glu Gly Ala Tyr Leu Glu Phe Phe 585 590 595 600 He Asp Asn He Pro Tyr Ser Met Glu Tyr Glu He Leu He Arg Tyr Glu Pro Gin Leu 605 610 615 620 Pro Asp His Trp Glu Lys Ala Val He Thr Val Gin Arg Pro Gly Lys He Pro Ala Ser 625 630 635 640 Ser Arg Cys Gly Asn Thr Val Pro Asp Asp Asp Asn Gin Val Val Ser Leu Ser Pro Gly 645 650 655 660 Ser Arg Tyr Val Val Leu Pro Arg Pro Val Cys Phe Glu Lys Gly Met Asn Tyr Thr Val 665 670 675 680 Arg Leu Glu Leu Pro Gin Tyr Thr Ala Ser Gly Ser Asp Val Glu Ser Pro Tyr Thr Phe 685 690 695 700 He Asp Ser Leu Val Leu Met Pro Tyr Cys Lys Ser Leu Asp He Phe Thr Val Gly Gly 705 710 715 720 Ser Gly Asp Gly Glu Val Thr Asn Ser Ala Trp Glu Thr Phe Gin Arg Tyr Arg Cys Leu 725 730 735 740 Glu Asn Ser Arg Ser Val Val Lys Thr Pro Met Thr Asp Val Cys Arg Asn He He Phe 745 750 755 760 Ser He Ser Ala Leu He His Gin Thr Gly Leu Ala Cys Glu Cys Asp Pro Gin Gly Ser 765 770 775 780 Leu Ser Ser Val Cys Asp Pro Asn Gly Gly Gin Cys Gin Cys Arg Pro Asn Val Val Gly 785 790 795 800 Arg Thr Cys Asn Arg Cys Ala Pro Gly Thr Phe Gly Phe Gly Pro Asn Gly Cys Lys Pro 805 810 815 820 Cys Asp Cys His Leu Gin Gly Ser Ala Ser Ala Phe Cys Asp Ala He Thr Gly Gin Cys 825 830 835 840 His Cys Phe Gin Gly He Tyr Ala Arg Gin Cys Asp Arg Cys Leu Pro Gly Tyr Trp Gly 845 850 855 860 Phe Pro Ser Cys Gin Pro Cys Gin Cys Asn Gly His Ala Leu Asp Cys Asp Thr Val Thr 865 870 875 880 Gly Glu Cys Leu Ser Cys Gin Asp Tyr Thr Thr Gly His Asn Cys Glu Arg Cys Leu Ala 885 890 895 900 Gly Tyr Tyr Gly Asp Pro He He Gly Ser Gly Asp His Cys Arg Pro Cys Pro Cys Pro 905 910 915 920 Asp Gly Pro Asp Ser Gly Arg Gin Phe Ala Arg Ser Cys Tyr Gin Asp Pro Val Thr Leu 925 930 935 940 Gin Leu Ala Cys Val Cys Asp Pro Gly Tyr He Gly Ser Arg Cys Asp Asp Cys Ala Ser 945 950 955 960 Gly Phe Phe Gly Asn Pro Ser Asp Phe Gly Gly Ser Cys Gin Pro Cys Gin Cys His His 965 970 975 980 Asn He Asp Thr Thr Asp Pro Glu Ala Cys Asp Lys Asp Thr Gly Arg Cys Leu Lys Cys 985 990 995 1000 Leu Tyr His Thr Glu Gly Asp His Cys Gin Leu Cys Gin Tyr Gly Tyr Tyr Gly Asp Ala 1005 1010 1015 1020 Leu Arg Gin Asp Cys Arg Lys Cys Val Cys Asn Tyr Leu Gly Thr Val Lys Glu His Cys 1025 1030 1035 1040 Asn Gly Ser Asp Cys His Cys Asp Lys Ala Thr Gly Gin Cys Ser Cys Leu Pro Asn Val 1045 1050 1055 1060 He Gly Gin Asn Cys Asp Arg Cys Ala Pro Asn Thr Trp Gin Leu Ala Ser Gly Thr Gly 1065 1070 1075 1080 Cys Gly Pro Cys Asn Cys Asn Ala Ala His Ser Phe Gly Pro Ser Cys Asn Glu Phe Thr 1085 1090 1095 1100 Gly Gin Cys Gin Cys Met Pro Gly Phe Gly Gly Arg Thr Cys Ser Glu Cys Gin Glu Leu 1105 1110 1115 1120 Phe Trp Gly Asp Pro Asp Val Glu Cys Arg Ala Cys Asp Cys Asp Pro Arg Gly He Glu 1125 1130 1135 1140 Thr Pro Gin Cys Asp Gin Ser Thr Gly Gin Cys Val Cys Val Glu Gly Val Glu Gly Pro 1145 1150 1155 1160 Arg Cys Asp Lys Cys Thr Arg Gly Tyr Ser Gly Val Phe Pro Asp Cys Thr Pro Cys His 1165 1170 1175 1180 Gin Cys Phe Ala Leu Trp Asp Ala He He Gly Glu Leu Thr Asn Arg Thr His Lys Phe 1185 1190 1195 1200 Leu Glu Lys Ala Lys Ala Leu Lys He Ser Gly Val He Gly Pro Tyr Arg Glu Thr Val 1205 1210 1215 1220 Asp Ser Val Glu Lys Lys Val Asn Glu He Lys Asp He Leu Ala Gin Ser Pro Ala Ala 1225 1230 1235 1240 Glu Pro Leu Lys Asn He Gly He Leu Phe Glu Glu Ala Glu Lys Leu Thr Lys Asp Val 1245 1250 1255 1260 Thr Glu Lys Met Ala Gin Val Glu Val Lys Leu Thr Asp Thr Ala Ser Gin Ser Asn Ser 1265 1270 1275 1280 Thr Ala Gly Glu Leu Gly Ala Leu Gin Ala Glu Ala Glu Ser Leu Asp Lys Thr Val Lys 1285 1290 1295 1300 Glu Leu Ala Glu Gin Leu Glu Phe He Lys Asn Ser Asp He Gin Gly Ala Leu Asp Ser 1305 1310 1315 1320 He Thr Lys Tyr Phe Gin Met Ser Leu Glu Ala Glu Lys Arg Val Asn Ala Ser Thr Thr 1325 1330 1335 1340 Asp Pro Asn Ser Thr Val Glu Gin Ser Ala Leu Thr Arg Asp Arg Val Glu Asp Leu Met 1345 1350 1355 1360 Leu Glu Arg Glu Ser Pro Phe Lys Glu Gin Gin Glu Glu Gin Ala Arg Leu Leu Asp Glu 1365 1370 1375 1380 Leu Ala Gly Lys Leu Gin Ser Leu Asp Leu Ser Ala Ala Ala Gin Met Thr Cys Gly Thr 1385 1390 1395 1400 Pro Pro Gly Ala Asp Cys Ser Glu Ser Glu Cys Gly Gly Pro Asn Cys Arg Thr Asp Glu 1405 1410 1415 1420 Gly Glu Lys Lys Cys Gly Gly Pro Gly Cys Gly Gly Leu Val Thr Val Ala His Ser Ala 1425 1430 1435 1440 Trp Gin Lys Ala Met Asp Phe Asp Arg Asp Val Leu Ser Ala Leu Ala Glu Val Glu Gin 1445 1450 1455 1460 Leu Ser Lys Met Val Ser Glu Ala Lys Val Arg Ala Asp Glu Ala Lys Gin Asn Ala Gin 1465 1470 1475 1480 Asp Val Leu Leu Lys Thr Asn fcla Thr Lys Glu Lys Val Asp Lys Ser Asn Glu Asp Leu 1485 1490 1495 1500 Arg Asn Leu He Lys Gin He Arg Asn Phe Leu Thr Glu Asp Ser Ala Asp Leu Asp Ser 1505 1510 1515 1520 He Glu Ala Val Ala Asn Glu Val Leu Lys Ser Gly Asn Ala Ser Thr Pro Gin Gin Leu 1525 1530 1535 1540 Gin Asn Leu Thr Glu Asp He Arg Glu Arg Val Glu Thr Leu Ser Gin Val Glu Val He 1545 1550 1555 1560 Leu Gin Gin Ser Ala Ala Asp He Ala Arg Ala Glu Leu Leu Leu Glu Glu Ala Lys Arg 1565 1570 1575 1580 Ala Ser Lys Ser Ala Thr Asp Val Lys Val Thr Ala Asp Met Val Lys Glu Ala Leu Glu 1585 1590 1595 1600 Glu Ala Glu Lys Ala Gin Val Ala Ala Glu Lys Ala He Lys Gin Ala Asp Glu Asp He 1605 1610 1615 1620 Gin Gly Thr Gin Asn Leu Leu Thr Ser He Glu Ser Glu Thr Ala Ala Ser Glu Glu Thr 1625 1630 1635 1640 Leu Thr Asn Ala Ser Gin Arg He Ser Lys Leu Glu Arg Asn Val Glu Glu Leu Lys Arg 1645 1650 1655 1660 Lys Ala Ala Gin Asn Ser Gly Glu Ala Glu Tyr He Glu Lys Val Val Tyr Ser Val Lys 1665 1670 1675 1680 Gin Asn Ala Asp Asp Val Lys Lys Thr Leu Asp Gly Glu Leu Asp Glu Lys Tyr Lys Lys 1685 1690 1695 1700 Val Glu Ser Leu He Ala Gin Lys Thr Glu Glu Ser Ala Asp Ala Arg Arg Lys Ala Glu 1705 1710 1715 1720 Leu Leu Gin Asn Glu Ala Lys Thr Leu Leu Ala Gin Ala Asn Ser Lys Leu Gin Leu Leu 1725 1730 1735 1740 Glu Asp Leu Glu Arg Lys Tyr Glu Asp Asn Gin Lys Tyr Leu Glu Asp Lys Ala Gin Glu 1745 1750 1755 1760 Leu Val Arg Leu Glu Gly Glu Val Arg Ser Leu Leu Lys Asp He Ser Glu Lys Val Ala 1765 1770 1775 1780 Val Tyr Ser Thr Cys Leu 1785 INFORMATION FOR SEQ ID NO: 8: SEQUENCE CHARACTERISTICS (A) LENGTH: 1801 AMINO ACIDS (B) TYPE: AMINO ACID (C) STRANDEDNESS: (D) TOPOLOGY: LINEAR (E) AMINO ACID NUMBERING ACCORDING TO TRANSLATION OF GENEBANK ACCESSION NUMBER P15800; MOLECULAR TYPE: PROTEIN SEQUENCE DESCRIPTION: SEQ ID NO 8: Met Glu Trp Ala Ser Gly Lys Pro Gly Arg Gly Arg Gin Gly Gin Pro Val Pro Trp Glu 1 5 10 15 20 Leu Arg Leu Gly Leu Leu Leu Ser Val Leu Ala Ala Thr Leu Ala Gin Val Pro Ser Leu 25 30 35 40 Asp Val Pro Gly Cys Ser Arg Gly Ser Cys Tyr Pro Ala Thr Gly Asp Leu Leu Val Gly 45 50 55 60 Arg Ala Asp Arg Leu Thr Ala Ser Ser Thr Cys Gly Leu His Ser Pro Gin Pro Tyr Cys 65 70 75 80 He Val Ser His Leu Gin Asp Glu Lys Lys Cys Phe Leu Cys Asp Ser Arg Arg Pro Phe 85 90 95 100 Ser Ala Arg Asp Asn Pro Asn Ser His Arg He Gin Asn Val Val Thr Ser Phe Ala Pro 105 110 115 120 Gin Arg Arg Thr Ala Trp Trp Gin Ser Glu Asn Gly Val Pro Met Val Thr He Gin Leu 125 130 135 140 Asp Leu Glu Ala Glu Phe His Phe Thr His Leu He Met Thr Phe Lys Thr Phe Arg Pro 145 150 155 160 Ala Ala Met Leu Val Glu Arg Ser Ala Asp Phe Gly Arg Thr Trp Arg Val Tyr Arg Tyr 165 170 175 180 Phe Ser Tyr Asp Cys Gly Ala Asp Phe Pro Gly He Pro Leu Ala Pro Pro Arg Arg Trp 185 190 195 200 Asp Asp Val Val Cys Glu Ser Arg Tyr Ser Glu He Glu Pro Ser Thr Glu Gly Glu Val 205 210 215 220 He Tyr Arg Val Leu Asp Pro Ala He Pro He Pro Asp Pro Tyr Ser Ser Arg He Gin 225 230 235 240 Asn Leu Leu Lys He Thr Asn Leu Arg Val Asn Leu Thr Arg Leu His Thr Leu Gly Asp 245 250 255 260 Asn Leu Leu Asp Pro Arg Arg Glu He Arg Glu Lys Tyr Tyr Tyr Ala Leu Tyr Glu Leu 265 270 275 280 Val He Arg Gly Asn Cys Phe Cys Tyr Gly His Ala Ser Gin Cys Ala Pro Ala Pro Gly 285 290 295 300 Ala Pro Ala His Ala Glu Gly Met Val His Gly Ala Cys He Cys Lys His Asn Thr Arg 305 310 315 320 Gly Leu Asn Cys Glu Gin Cys Gin Asp Phe Tyr Gin Asp Leu Pro Trp His Pro Ala Glu 325 330 335 340 Asp Gly His Thr His Ala Cys Arg Lys Cys Glu Cys Asn Gly His Ser His Ser Cys His 345 350 355 360 Phe Asp Met Ala Val Tyr Leu Ala Ser Gly Asn Val Ser Gly Gly Val Cys Asp Gly Cys 365 370 375 380 Gin His Asn Thr Ala Gly Arg His Cys Glu Leu Cys Arg Pro Phe Phe Tyr Arg Asp Pro 385 390 395 400 Thr Lys Asp Met Arg Asp Pro Ala Ala Cys Arg Pro Cys Asp Cys Asp Pro Met Gly Ser 405 410 415 420 Gin Asp Gly Gly Arg Cys Asp Ser His Asp Asp Pro Val Leu Gly Leu Val Ser Gly Gin 425 430 435 440 Cys Arg Cys Lys Glu His Val Val Gly Thr Arg Cys Gin Gin Cys Arg Asp Gly Phe Phe 445 450 455 460 Gly Leu Ser Ala Ser Asn Pro Arg Gly Cys Gin Arg Cys Gin Cys Asn Ser Arg Gly Thr 465 470 475 480 Val Pro Gly Gly Thr Pro Cys Asp Ser Ser Ser Gly Thr Cys Phe Cys Lys Arg Leu Val 485 490 495 500 Thr Gly Asp Gly Cys Asp Arg Cys Leu Pro Gly His Trp Gly Leu Ser His Asp Leu Leu 505 510 515 520 Gly Cys Arg Pro Cys Asp Cys Asp Val Gly Gly Ala Leu Asp Pro Gin Cys Asp Glu Ala 525 530 535 540 Thr Gly Gin Cys Pro Cys Arg Pro His Met He Gly Arg Arg Cys Glu Gin Val Gin Pro 545 550 555 560 Gly Tyr Phe Arg Pro Phe Leu Asp His Leu Thr Trp Glu Ala Glu Gly Ala His Gly Gin 565 570 575 580 Val Leu Glu Val Val Glu Arg Leu Val Thr Asn Arg Glu Thr Pro Ser Trp Thr Gly Val 585 590 595 600 Gly Phe Val Arg Leu Arg Glu Gly Gin Glu Val Glu Phe Leu Val Thr Ser Leu Pro Arg 605 610 615 620 Ala Met Asp Tyr Asp Leu Leu Leu Arg Trp Glu Pro Gin Val Pro Glu Gin Trp Ala Glu 625 630 635 640 Leu Glu Leu Val Val Gin Arg Pro Gly Pro Val Ser Ala His Ser Pro Cys Gly His Val 645 650 655 660 Leu Pro Arg Asp Asp Arg He Gin Gly Met Leu His Pro Asn Thr Arg Val Leu Val Phe 665 670 675 680 Pro Arg Pro Val Cys Leu Glu Pro Gly Leu Ser Tyr Lys Leu Lys Leu Lys Leu Thr Gly 685 690 695 700 Thr Gly Gly Arg Ala His Pro Glu Thr Pro Tyr Ser Gly Ser Gly He Leu He Asp Ser 705 710 715 720 Leu Val Leu Gin Pro His Val Leu Met Leu Glu Met Phe Ser Gly Gly Asp Ala Ala Ala 725 730 735 740 Leu Glu Arg Arg Thr Thr Phe Glu Arg Tyr Arg Cys His Glu Glu Gly Leu Met Pro Ser 745 750 755 760 Lys Thr Pro Leu Ser Glu Ala Cys Val Pro Leu Leu He Ser Ala Ser Ser Leu Val Tyr 765 770 775 780 Asn Gly Ala Leu Pro Cys Gin Cys Asp Pro Gin Gly Ser Leu Ser Ser Glu Cys Asn Pro 785 790 795 800 His Gly Gly Gin Cys Arg Cys Lys Pro Gly Val Val Gly Arg Arg Cys Asp Ala Cys Ala 805 810 815 820 Thr Gly Tyr Tyr Gly Phe Gly Pro Ala Gly Cys Gin Ala Cys Gin Cys Ser Pro Asp Gly 825 830 835 840 Ala Leu Ser Ala Leu Cys Glu Gly Thr Ser Gly Gin Cys Leu Cys Arg Thr Gly Ala Phe 845 850 855 860 Gly Leu Arg Cys Asp His Cys Gin Arg Gly Gin Trp Gly Phe Pro Asn Cys Arg Pro Cys 865 870 875 880 Val Cys Asn Gly Arg Ala Asp Glu Cys Asp Ala His Thr Gly Ala Cys Leu Gly Cys Arg 885 890 895 900 Asp Tyr Thr Gly Gly Glu His Cys Glu Arg Cys He Ala Gly Phe His Gly Asp Pro Arg 905 910 915 920 Leu Pro Tyr Gly Gly Gin Cys Arg Pro Cys Pro Cys Pro Glu Gly Pro Gly Ser Gin Arg 925 930 935 940 His Phe Ala Thr Ser Cys His Arg Asp Gly Tyr Ser Gin Gin He Val Cys His Cys Arg 945 950 955 960 Ala Gly Tyr Thr Gly Leu Arg Cys Glu Ala Cys Ala Pro Gly His Phe Gly Asp Pro Ser 965 970 975 980 Lys Pro Gly Gly Arg Cys Gin Leu Cys Glu Cys Ser Gly Asn He Asp Pro Thr Asp Pro 985 990 995 1000 Gly Ala Cys Asp Pro His Thr Gly Gin Cys Leu Arg Cys Leu His His Thr Glu Gly Pro 1005 1010 1015 1020 His Cys Gly His Cys Lys Pro Gly Phe His Gly Gin Ala Ala Arg Gin Ser Cys His Arg 1025 1030 1035 1040 Cys Thr Cys Asn Leu Leu Gly Thr Asp Pro Gin Arg Cys Pro Ser Thr Asp Leu Cys His 1045 1050 1055 1060 Cys Asp Pro Ser Thr Gly Gin Cys Pro Cys Leu Pro His Val Gin Gly Leu Ser Cys Asp 1065 1070 1075 1080 Arg Cys Ala Pro Asn Phe Trp Asn Phe Thr Ser Gly Arg Gly Cys Gin Pro Cys Ala Cys 1085 1090 1095 1100 His Pro Ser Arg Ala Arg Gly Pro Thr Cys Asn Glu Phe Thr Gly Gin Cys His Cys His 1105 1110 1115 1120 Ala Gly Phe Gly Gly Arg Thr Cys Ser Glu Cys Gin Glu Leu His Trp Gly Asp Pro Gly 1125 1130 1135 1140 Leu Gin Cys Arg Ala Cys Asp Cys Asp Pro Arg Gly He Asp Lys Pro Gin Cys His Arg 1145 1150 1155 1160 Ser Thr Gly His Cys Ser Cys Arg Pro Gly Val Ser Gly Val Arg Cys Asp Gin Cys Ala 1165 1170 1175 1180 Arg Gly Phe Ser Gly Val Phe Pro Ala Cys His Pro Cys His Ala Cys Phe Gly Asp Trp 1185 1190 1195 1200 Asp Arg Val Val Gin Asp Leu Ala Ala Arg Thr Arg Arg Leu Glu Gin Trp Ala Gin Glu 1205 1210 1215 1220 Leu Gin Gin Thr Gly Val Leu Gly Ala Phe Glu Ser Ser Phe Leu Asn Leu Gin Gly Lys 1225 1230 1235 1240 Leu Gly Met Val Gin Ala He Val Ala Ala Arg Asn Thr Ser Ala Ala Ser Thr Ala Lys 1245 1250 1255 1260 Leu Val Glu Ala Thr Glu Gly Leu Arg His Glu He Gly Lys Thr Thr Glu Arg Leu Thr 1265 1270 1275 1280 Gin Leu Glu Ala Glu Leu Thr Asp Val Gin Asp Glu Asn Phe Asn Ala Asn His Ala Leu 1285 1290 1295 1300 Ser Gly Leu Glu Arg Asp Gly Leu Ala Leu Asn Leu Thr Leu Arg Gin Leu Asp Gin His 1305 1310 1315 1320 Leu Asp He Leu Lys His Ser Asn Phe Leu Gly Ala Tyr Asp Ser He Arg His Ala His 1325 1330 1335 1340 Ser Gin Ser Thr Glu Ala Glu Arg Arg Ala Asn Ala Ser Thr Phe Ala He Pro Ser Pro 1345 1350 1355 1360 Val Ser Asn Ser Ala Asp Thr Arg Arg Arg Ala Glu Val Leu Met Gly Ala Gin Arg Glu 1365 1370 1375 1380 Asn Phe Asn Arg Gin His Leu Ala Asn Gin Gin Ala Leu Gly Arg Leu Ser Thr His Thr 1385 1390 1395 1400 His Thr Leu Ser Leu Thr Gly Val Asn Glu Leu Val Cys Gly Ala Pro Gly Asp Ala Pro 1405 1410 1415 1420 Cys Ala Thr Ser Pro Cys Gly Gly Ala Gly Cys Arg Asp Glu Asp Gly Gin Pro Arg Cys 1425 1430 1435 1440 Gly Gly Leu Gly Cys Ser Gly Ala Ala Ala Thr Ala Asp Leu Ala Leu Gly Arg Ala Arg 1445 1450 1455 1460 His Thr Gin Ala Glu Leu Gin Arg Ala Leu Val Glu Gly Gly Gly He Leu Ser Arg Val 1465 1470 1475 1480 Ser Glu Thr Arg Arg Gin Ala Glu Glu Ala Gin Gin Arg Ala Gin Ala Ala Leu Asp Lys 1485 1490 1495 1500 Ala Asn Ala Ser Arg Gly Gin Val Glu Gin Ala Asn Gin Glu Leu Arg Glu Leu He Gin 1505 1510 1515 1520 Asn Val Lys Asp Phe Leu Ser Gin Glu Gly Ala Asp Pro Asp Ser He Glu Met Val Ala 1525 1530 1535 1540 Thr Arg Val Leu Asp He Ser He Pro Ala Ser Pro Glu Gin He Gin Arg Leu Ala Ser 1545 1550 1555 1560 Glu He Ala Glu Arg Val Arg Ser Leu Ala Asp Val Asp Thr He Leu Ala His Thr Met 1565 1570 1575 1580 Gly Asp Val Arg Arg Ala Glu Gin Leu Leu Gin Asp Ala Gin Arg Ala Arg Ser Arg Ala 1585 1590 1595 1600 Glu Gly Glu Arg Gin Lys Ala Glu Thr Val Gin Ala Ala Leu Glu Glu Ala Gin Arg Ala 1605 1610 1615 1620 Gin Gly Ala Ala Gin Gly Ala He Arg Gly Ala Val Val Asp Thr Lys Asn Thr Glu Gin 1625 1630 1635 1640 Thr Leu Gin Gin Val Gin Glu Arg Met Ala Gly Thr Glu Gin Ser Leu Asn Ser Ala Ser 1645 1650 1655 1660 Glu Arg Ala Arg Gin Leu His Ala Leu Leu Glu Ala Leu Lys Leu Lys Arg Ala Gly Asn 1665 1670 1675 1680 Ser Leu Ala Ala Ser Thr Ala Glu Glu Thr Ala Gly Ser Ala Gin Ser Arg Ala Arg Glu 1685 1690 1695 1700 Ala Glu Lys Gin Leu Arg Glu Gin Val Gly Asp Gin Tyr Gin Thr Val Arg Ala Leu Ala 1705 1710 1715 1720 Glu Arg Lys Ala Glu Gly Val Leu Ala Ala Gin Ala Arg Ala Glu Gin Leu Arg Asp Glu 1725 1730 1735 1740 Ala Arg Gly Leu Leu Gin Ala Ala Gin Asp Lys Leu Gin Arg Leu Gin Glu Leu Glu Gly 1745 1750 1755 1760 Thr Tyr Glu Glu Asn Glu Arg Glu Leu Glu Val Lys Ala Ala Gin Leu Asp Gly Leu Glu 1765 1770 1775 1780 Ala Arg Met Arg Ser Val Leu Gin Ala He Asn Leu Gin Val Gin He Tyr Asn Thr Cys 1785 1790 1795 1800 Gin INFORMATION FOR SEQ ID NO: 9: SEQUENCE CHARACTERISTICS (A) LENGTH: 1798 AMINO ACIDS (B) TYPE: AMINO ACID (C) STRANDEDNESS: (D) TOPOLOGY: LINEAR (E) AMINO ACID NUMBERING ACCORDING TO TRANSLATION OF GENEBANK ACCESSION NUMBER P55268; MOLECULAR TYPE: PROTEIN SEQUENCE DESCRIPTION: SEQ ID NO 9: Met Glu Leu Thr Ser Arg Glu Arg Gly Arg Gly Gin Pro Leu Pro Trp Glu Leu Arg Leu 1 5 10 15 20 Gly Leu Leu Leu Ser Val Leu Ala Ala Thr Leu Ala Gin Ala Pro Ala Pro Asp Val Pro 25 30 35 40 Gly Cys Ser Arg Gly Ser Cys Tyr Pro Ala Thr Gly Asp Leu Leu Val Gly Arg Ala Asp 45 50 55 60 Arg Leu Thr Ala Ser Ser Thr Cys Gly Leu Asn Gly Pro Gin Pro Tyr Cys He Val Ser 65 70 75 80 His Leu Gin Asp Glu Lys Lys Cys Phe Leu Cys Asp Ser Arg Arg Pro Phe Ser Ala Arg 85 90 95 100 Asp Asn Pro His Ser His Arg He Gin Asn Val Val Thr Ser Phe Ala Pro Gin Arg Arg 105 110 115 120 Ala Ala Trp Trp Gin Ser Glu Asn Gly He Pro Ala Val Thr He Gin Leu Asp Leu Glu 125 130 135 140 Ala Glu Phe His Phe Thr His Leu He Met Thr Phe Lys Thr Phe Arg Pro Ala Ala Met 145 150 155 160 Leu Val Glu Arg Ser Ala Asp Phe Gly Arg Thr Trp His Val Tyr Arg Tyr Phe Ser Tyr 165 170 175 180 Asp Cys Gly Ala Asp Phe Pro Gly Val Pro Leu Ala Pro Pro Arg His Trp Asp Asp Val 185 190 195 200 Val Cys Glu Ser Arg Tyr Ser Glu He Glu Pro Ser Thr Glu Gly Glu Val He Tyr Arg 205 210 215 220 Val Leu Asp Pro Ala He Pro He Pro Asp Pro Tyr Ser Ser Arg He Gin Asn Leu Leu 225 230 235 240 Lys He Thr Asn Leu Arg Val Asn Leu Thr Arg Leu His Thr Leu Gly Asp Asn Leu Leu 245 250 255 260 Asp Pro Arg Arg Glu He Arg Glu Lys Tyr Tyr Tyr Ala Leu Tyr Glu Leu Val Val Arg 265 270 275 280 Gly Asn Cys Phe Cys Tyr Gly His Ala Ser Glu Cys Ala Pro Ala Pro Gly Ala Pro Ala 285 290 295 300 His Ala Glu Gly Met Val His Gly Ala Cys He Cys Lys His Asn Thr Arg Gly Leu Asn 305 310 315 320 Cys Glu Gin Cys Gin Asp Phe Tyr Arg Asp Leu Pro Trp Arg Pro Ala Glu Asp Gly His 325 330 335 340 Ser His Ala Cys Arg Lys Cys Glu Cys His Gly His Thr His Ser Cys His Phe Asp Met 345 350 355 360 Ala Val Tyr Leu Ala Ser Gly Asn Val Ser Gly Gly Val Cys Asp Gly Cys Gin His Asn 365 370 375 380 Thr Ala Gly Arg His Cys Glu Leu Cys Arg Pro Phe Phe Tyr Arg Asp Pro Thr Lys Asp 385 390 395 400 Leu Arg Asp Pro Ala Val Cys Arg Ser Cys Asp Cys Asp Pro Met Gly Ser Gin Asp Gly 405 410 415 420 Gly Arg Cys Asp Ser His Asp Asp Pro Ala Leu Gly Leu Val Ser Gly Gin Cys Arg Cys 425 430 435 440 Lys Glu His Val Val Gly Thr Arg Cys Gin Gin Cys Arg Asp Gly Phe Phe Gly Leu Ser 445 450 455 460 He Ser Asp Arg Leu Gly Cys Arg Arg Cys Gin Cys Asn Ala Arg Gly Thr Val Pro Gly 465 470 475 480 Ser Thr Pro Cys Asp Pro Asn Ser Gly Ser Cys Tyr Cys Lys Arg Leu Val Thr Gly Arg 485 490 495 500 Gly Cys Asp Arg Cys Leu Pro Gly His Trp Gly Leu Ser His Asp Leu Leu Gly Cys Arg 505 510 515 520 Pro Cys Asp Cys Asp Val Gly Gly Ala Leu Asp Pro Gin Cys Asp Glu Gly Thr Gly Gin 525 530 535 540 Cys His Cys Arg Gin His Met Val Gly Arg Arg Cys Glu Gin Val Gin Pro Gly Tyr Phe 545 550 555 560 Arg Pro Phe Leu Asp His Leu He Trp Glu Ala Glu Asp Thr Arg Gly Gin Val Leu Asp 565 570 575 580 Val Val Glu Arg Leu Val Thr Pro Gly Glu Thr Pro Ser Trp Thr Gly Ser Gly Phe Val 585 590 595 600 Arg Leu Gin Glu Gly Gin Thr Leu Glu Phe Leu Val Ala Ser Val Pro Lys Ala Met Asp 605 610 615 620 Tyr Asp Leu Leu Leu Arg Leu Glu Pro Gin Val Pro Glu Gin Trp Ala Glu Leu Glu Leu 625 630 635 640 He Val Gin Arg Pro Gly Pro Val Pro Ala His Ser Leu Cys Gly His Leu Val Pro Lys 645 650 655 660 Asp Asp Arg He Gin Gly Thr Leu Gin Pro His Ala Arg Tyr Leu He Phe Pro Asn Pro 665 670 675 680 Val Cys Leu Glu Pro Gly He Ser Tyr Lys Leu His Leu Lys Leu Val Arg Thr Gly Gly 685 690 695 700 Ser Ala Gin Pro Glu Thr Pro Tyr Ser Gly Pro Gly Leu Leu He Asp Ser Leu Val Leu 705 710 715 720 Leu Pro Arg Val Leu Val Leu Glu Met Phe Ser Gly Gly Asp Ala Ala Ala Leu Glu Arg 725 730 735 740 Gin Ala Thr Phe Glu Arg Tyr Gin Cys His Glu Glu Gly Leu Val Pro Ser Lys Thr Ser 745 750 755 760 Pro Ser Glu Ala Cys Ala Pro Leu Leu He Ser Leu Ser Thr Leu He Tyr Asn Gly Ala 765 770 775 780 Leu Pro Cys Gin Cys Asn Pro Gin Gly Ser Leu Ser Ser Glu Cys Asn Pro His Gly Gly 785 790 795 800 Gin Cys Leu Cys Lys Pro Gly Val Val Gly Arg Arg Cys Asp Leu Cys Ala Pro Gly Tyr 805 810 815 820 Tyr Gly Phe Gly Pro Thr Gly Cys Gin Ala Cys Gin Cys Ser His Glu Gly Ala Leu Ser 825 830 835 840 Ser Leu Cys Glu Lys Thr Ser Gly Gin Cys Leu Cys Arg Thr Gly Ala Phe Gly Leu Arg 845 850 855 860 Cys Asp Arg Cys Gin Arg Gly Gin Trp Gly Phe Pro Ser Cys Arg Pro Cys Val Cys Asn 865 870 875 880 Gly His Ala Asp Glu Cys Asn Thr His Thr Gly Ala Cys Leu Gly Cys Arg Asp His Thr 885 890 895 900 Gly Gly Glu His Cys Glu Arg Cys He Ala Gly Phe His Arg Asp Pro Arg Leu Pro Tyr 905 910 915 920 Gly Gly Gin Cys Arg Pro Cys Pro Cys Pro Glu Gly Pro Gly Ser Gin Arg His Phe Ala 925 930 935 940 Thr Ser Cys His Gin Asp Glu Tyr Ser Gin Gin He Val Cys His Cys Arg Ala Gly Tyr 945 950 955 960 Thr Gly Leu Arg Cys Glu Ala Cys Ala Pro Gly His Phe Gly Asp Pro Ser Arg Pro Gly 965 970 975 980 Gly Arg Cys Gin Leu Cys Glu Cys Ser Gly Asn He Asp Pro Met Asp Pro Asp Ala Cys 985 990 995 1000 Asp Pro His Thr Gly Gin Cys Leu Arg Cys Leu His His Thr Glu Gly Pro His Cys Ala 1005 1010 1015 1020 His Cys Lys Pro Gly Phe His Gly Gin Ala Ala Arg Gin Ser Cys His Arg Cys Thr Cys 1025 1030 1035 1040 Asn Leu Leu Gly Thr Asn Pro Gin Gin Cys Pro Ser Pro Asp Gin Cys His Cys Asp Pro 1045 1050 1055 1060 Ser Ser Gly Gin Cys Pro Cys Leu Pro Asn Val Gin Gly Pro Ser Cys Asp Arg Cys Ala 1065 1070 1075 1080 Pro Asn Phe Trp Asn Leu Thr Ser Gly His Gly Cys Gin Pro Cys Ala Cys His Pro Ser 1085 1090 1095 1100 Arg Ala Arg Gly Pro Thr Cys Asn Glu Phe Thr Gly Gin Cys His Cys Arg Ala Gly Phe 1105 1110 1115 1120 Gly Gly Arg Thr Cys Ser Glu Cys Gin Glu Leu His Trp Gly Asp Pro Gly Leu Gin Cys 1125 1130 1135 1140 His Ala Cys Asp Cys Asp Ser Arg Gly He Asp Thr Pro Gin Cys His Arg Phe Thr Gly 1145 1150 1155 1160 His Cys Ser Cys Arg Pro Gly Val Ser Gly Val Arg Cys Asp Gin Cys Ala Arg Gly Phe 1165 1170 1175 1180 Ser Gly He Phe Pro Ala Cys His Pro Cys His Ala Cys Phe Gly Asp Trp Asp Arg Val 1185 1190 1195 1200 Val Gin Asp Leu Ala Ala Arg Thr Gin Arg Leu Glu Gin Arg Ala Gin Glu Leu Gin Gin 1205 1210 1215 1220 Thr Gly Val Leu Gly Ala Phe Glu Ser Ser Phe Trp His Met Gin Glu Lys Leu Gly He 1225 1230 1235 1240 Val Gin Gly He Val Gly Ala Arg Asn Thr Ser Ala Ala Ser Thr Ala Gin Leu Val Glu 1245 1250 1255 1260 Ala Thr Glu Glu Leu Arg Arg Glu He Gly Glu Ala Thr Glu His Leu Thr Gin Leu Glu 1265 1270 1275 1280 Ala Asp Leu Thr Asp Val Gin Asp Glu Asn Phe Asn Ala Asn His Ala Leu Ser Gly Leu 1285 1290 1295 1300 Glu Arg Asp Arg Leu Ala Leu Asn Leu Thr Leu Arg Gin Leu Asp Gin His Leu Asp Leu 1305 1310 1315 1320 Leu Lys His Ser Asn Phe Leu Gly Ala Tyr Asp Ser He Arg His Ala His Ser Gin Ser 1325 1330 1335 1340 Ala Glu Ala Glu Arg Arg Ala Asn Thr Ser Ala Leu Ala Val Pro Ser Pro Val Ser Asn 1345 1350 1355 1360 Ser Ala Ser Ala Arg His Arg Thr Glu Ala Leu Met Asp Ala Gin Lys Glu Asp Phe Asn 1365 1370 1375 1380 Ser Lys His Met Ala Asn Gin Arg Ala Leu Gly Lys Leu Ser Ala His Thr His Thr Leu 1385 1390 1395 1400 Ser Leu Thr Asp He Asn Glu Leu Val Cys Gly Ala Pro Gly Asp Ala Pro Cys Ala Thr 1405 1410 1415 1420 Ser Pro Cys Gly Gly Ala Gly Cys Arg Asp Glu Asp Gly Gin Pro Arg Cys Gly Gly Leu 1425 1430 1435 1440 Ser Cys Asn Gly Ala Ala Ala Thr Ala Asp Leu Ala Leu Gly Arg Ala Arg His Thr Gin 1445 1450 1455 1460 Ala Glu Leu Gin Arg Ala Leu Ala Glu Gly Gly Ser He Leu Ser Arg Val Ala Glu Thr 1465 1470 1475 1480 Arg Arg Gin Ala Ser Glu Ala Gin Gin Arg Ala Gin Ala Ala Leu Asp Lys Ala Asn Ala 1485 1490 1495 1500 Ser Arg Gly Gin Val Glu Gin Ala Asn Gin Glu Leu Gin Glu Leu He Gin Ser Val Lys 1505 1510 1515 1520 Asp Phe Leu Asn Gin Glu Gly Ala Asp Pro Asp Ser He Glu Met Val Ala Thr Arg Val 1525 1530 1535 1540 Leu Glu Leu Ser He Pro Ala Ser Ala Glu Gin He Gin His Leu Ala Gly Ala He Ala 1545 1550 1555 1560 Glu Arg Val Arg Ser Leu Ala Asp Val Asp Ala He Leu Ala Arg Thr Val Gly Asp Val 1565 1570 1575 1580 Arg Arg Ala Glu Gin Leu Leu Gin Asp Ala Arg Arg Ala Arg Ser Trp Ala Glu Asp Glu 1585 1590 1595 1600 Lys Gin Lys Ala Glu Thr Val Gin Ala Ala Leu Glu Glu Ala Gin Arg Ala Gin Gly He 1605 1610 1615 1620 Ala Gin Gly Ala He Arg Gly Ala Val Ala Asp Thr Arg Asp Thr Glu Gin Thr Leu Tyr 1625 1630 1635 1640 Gin Val Gin Glu Arg Met Ala Gly Ala Glu Arg Ala Leu Ser Ser Ala Gly Glu Arg Ala 1645 1650 1655 1660 Arg Gin Leu Asp Ala Leu Leu Glu Ala Leu Lys Leu Lys Arg Ala Gly Asn Ser Leu Ala 1665 1670 1675 1680 Ala Ser Thr Ala Glu Glu Thr Ala Gly Ser Ala Gin Gly Arg Ala Gin Glu Ala Glu Gin 1685 1690 1695 1700 Leu Leu Arg Gly Pro Leu Gly Asp Gin Tyr Gin Thr Val Lys Ala Leu Ala Glu Arg Lys 1705 1710 1715 1720 Ala Gin Gly Val Leu Ala Ala Gin Ala Arg Ala Glu Gin Leu Arg Asp Glu Ala Arg Asp 1725 1730 1735 1740 Leu Leu Gin Ala Ala Gin Asp Lys Leu Gin Arg Leu Gin Glu Leu Glu Gly Thr Tyr Glu 1745 1750 1755 1760 Glu Asn Glu Arg Ala Leu Glu Ser Lys Ala Ala Gin Leu Asp Gly Leu Glu Ala Arg Met 1765 1770 1775 1780 Arg Ser Val Leu Gin Ala He Asn Leu Gin Val Gin He Tyr Asn Thr Cys Gin 1785 1790 1795 INFORMATION FOR SEQ ID NO: 10: SEQUENCE CHARACTERISTICS (A) LENGTH: 1607 AMINO ACIDS (B) TYPE: AMINO ACID (C) STRANDEDNESS: (D) TOPOLOGY: LINEAR (E) AMINO ACID NUMBERING ACCORDING TO TRANSLATION OF GENEBANK ACCESSION NUMBER P02468; MOLECULAR TYPE: PROTEIN SEQUENCE DESCRIPTION: SEQ ID NO 10: Met Thr Gly Gly Gly Arg Ala Ala Leu Ala Leu Gin Pro Arg Gly Arg Leu Trp Pro Leu 1 5 10 15 20 Leu Ala Val Leu Ala Ala Val Ala Gly Cys Val Arg Ala Ala Met Asp Glu Cys Ala Asp 25 30 35 40 Glu Gly Gly Arg Pro Gin Arg Cys Met Pro Glu Phe Val Asn Ala Ala Phe Asn Val Thr 45 50 55 60 Val Val Ala Thr Asn Thr Cys Gly Thr Pro Pro Glu Glu Tyr Cys Val Gin Thr Gly Val 65 70 75 80 Thr Gly Val Thr Lys Ser Cys His Leu Cys Asp Ala Gly Gin Gin His Leu Gin His Gly 85 90 95 100 Ala Ala Phe Leu Thr Asp Tyr Asn Asn Gin Ala Asp Thr Thr Trp Trp Gin Ser Gin Thr 105 110 115 120 Met Leu Ala Gly Val Gin Tyr Pro Asn Ser He Asn Leu Thr Leu His Leu Gly Lys Ala 125 130 135 140 Phe Asp He Thr Tyr Val Arg Leu Lys Phe His Thr Ser Arg Pro Glu Ser Phe Ala He 145 150 155 160 Tyr Lys Arg Thr Arg Glu Asp Gly Pro Trp He Pro Tyr Gin Tyr Tyr Ser Gly Ser Cys 165 170 175 180 Glu Asn Thr Tyr Ser Lys Ala Asn Arg Gly Phe He Arg Thr Gly Gly Asp Glu Gin Gin 185 190 195 200 Ala Leu Cys Thr Asp Glu Phe Ser Asp He Ser Pro Leu Thr Gly Gly Asn Val Ala Phe 205 210 215 220 Ser Thr Leu Glu Gly Arg Pro Ser Ala Tyr Asn Phe Asp Asn Ser Pro Val Leu Gin Glu 225 230 235 240 Trp Val Thr Ala Thr Asp He Arg Val Thr Leu Asn Arg Leu Asn Thr Phe Gly Asp Glu 245 250 255 260 Val Phe Asn Glu Pro Lys Val Leu Lys Ser Tyr Tyr Tyr Ala He Ser Asp Phe Ala Val 265 270 275 280 Gly Gly Arg Cys Lys Cys Asn Gly His Ala Ser Glu Cys Val Lys Asn Glu Phe Asp Lys 285 290 295 300 Leu Met Cys Asn Cys Lys His Asn Thr Tyr Gly Val Asp Cys Glu Lys Cys Leu Pro Phe 305 310 315 320 Phe Asn Asp Arg Pro Trp Arg Arg Ala Thr Ala Glu Ser Ala Ser Glu Ser Leu Pro Cys 325 330 335 340 Asp Cys Asn Gly Arg Ser Gin Glu Cys Tyr Phe Asp Pro Glu Leu Tyr Arg Ser Thr Gly 345 350 355 360 His Gly Gly His Cys Thr Asn Cys Arg Asp Asn Thr Asp Gly Ala Lys Cys Glu Arg Cys 365 370 375 380 Arg Glu Asn Phe Phe Arg Leu Gly Asn Thr Glu Ala Cys Ser Pro Cys His Cys Ser Pro 385 390 395 400 Val Gly Ser Leu Ser Thr Gin Cys Asp Ser Tyr Gly Arg Cys Ser Cys Lys Pro Gly Val 405 410 415 420 Met Gly Asp Lys Cys Asp Arg Cys Gin Pro Gly Phe His Ser Leu Thr Glu Ala Gly Cys 425 430 435 440 Arg Pro Cys Ser Cys Asp Leu Arg Gly Ser Thr Asp Glu Cys Asn Val Glu Thr Gly Arg 445 450 455 460 Cys Val Cys Lys Asp Asn Val Glu Gly Phe Asn Cys Glu Arg Cys Lys Pro Gly Phe Phe 465 470 475 480 Asn Leu Glu Ser Ser Asn Pro Lys Gly Cys Thr Pro Cys Phe Cys Phe Gly His Ser Ser 485 490 495 500 Val Cys Thr Asn Ala Val Gly Tyr Ser Val Tyr Asp He Ser Ser Thr Phe Gin He Asp 505 510 515 520 Glu Asp Gly Trp Arg Val Glu Gin Arg Asp Gly Ser Glu Ala Ser Leu Glu Trp Ser Ser 525 530 535 540 Asp Arg Gin Asp He Ala Val He Ser Asp Ser Tyr Phe Pro Arg Tyr Phe He Ala Pro 545 550 555 560 Val Lys Phe Leu Gly Asn Gin Val Leu Ser Tyr Gly Gin Asn Leu Ser Phe Ser Phe Arg 565 570 575 580 Val Asp Arg Arg Asp Thr Arg Leu Ser Ala Glu Asp Leu Val Leu Glu Gly Ala Gly Leu 585 590 595 600 Arg Val Ser Val Pro Leu He Ala Gin Gly Asn Ser Tyr Pro Ser Glu Thr Thr Val Lys 605 610 615 620 Tyr He Phe Arg Leu His Glu Ala Thr Asp Tyr Pro Trp Arg Pro Ala Leu Ser Pro Phe 625 630 635 640 Glu Phe Gin Lys Leu Leu Asn Asn Leu Thr Ser He Lys He Arg Gly Thr Tyr Ser Glu 645 650 655 660 Arg Thr Ala Gly Tyr Leu Asp Asp Val Thr Leu Gin Ser Ala Arg Pro Gly Pro Gly Val 665 670 675 680 Pro Ala Thr Trp Val Glu Ser Cys Thr Cys Pro Val Gly Tyr Gly Gly Gin Phe Cys Glu 685 690 695 700 Thr Cys Leu Pro Gly Tyr Arg Arg Glu Thr Pro Ser Leu Gly Pro Tyr Ser Pro Cys Val 705 710 715 720 Leu Cys Thr Cys Asn Gly His Ser Glu Thr Cys Asp Pro Glu Thr Gly Val Cys Asp Cys 725 730 735 740 Arg Asp Asn Thr Ala Gly Pro His Cys Glu Lys Cys Ser Asp Gly Tyr Tyr Gly Asp Ser 745 750 755 760 Thr Leu Gly Thr Ser Ser Asp Cys Gin Pro Cys Pro Cys Pro Gly Gly Ser Ser Cys Ala 765 770 775 780 He Val Pro Lys Thr Lys Glu Val Val Cys Thr His Cys Pro Thr Gly Thr Ala Gly Lys 785 790 795 800 Arg Cys Glu Leu Cys Asp Asp Gly Tyr Phe Gly Asp Pro Leu Gly Ser Asn Gly Pro Val 805 810 815 820 Arg Leu Cys Arg Pro Cys Gin Cys Asn Asp Asn He Asp Pro Asn Ala Val Gly Asn Cys 825 830 835 840 Asn Arg Leu Thr Gly Glu Cys Leu Lys Cys He Tyr Asn Thr Ala Gly Phe Tyr Cys Asp 845 850 855 860 Arg Cys Lys Glu Gly Phe Phe Gly Asn Pro Leu Ala Pro Asn Pro Ala Asp Lys Cys Lys 865 870 875 880 Ala Cys Ala Cys Asn Pro Tyr Gly Thr Val Gin Gin Gin Ser Ser Cys Asn Pro Val Thr 885 890 895 900 Gly Gin Cys Gin Cys Leu Pro His Val Ser Gly Arg Asp Cys Gly Thr Cys Asp Pro Gly 905 910 915 920 Tyr Tyr Asn Leu Gin Ser Gly Gin Gly Cys Glu Arg Cys Asp Cys His Ala Leu Gly Ser 925 930 935 940 Thr Asn Gly Gin Cys Asp He Arg Thr Gly Gin Cys Glu Cys Gin Pro Gly He Thr Gly 945 950 955 960 Gin His Cys Glu Arg Cys Glu Thr Asn His Phe Gly Phe Gly Pro Glu Gly Cys Lys Pro 965 970 975 980 Cys Asp Cys His His Glu Gly Ser Leu Ser Leu Gin Cys Lys Asp Asp Gly Arg Cys Glu 985 990 995 1000 Cys Arg Glu Gly Phe Val Gly Asn Arg Cys Asp Gin Cys Glu Glu Asn Tyr Phe Tyr Asn 1005 1010 1015 1020 Arg Ser Trp Pro Gly Cys Gin Glu Cys Pro Ala Cys Tyr Arg Leu Val Lys Asp Lys Ala 1025 1030 1035 1040 Ala Glu His Arg Val Lys Leu Gin Glu Leu Glu Ser Leu He Ala Asn Leu Gly Thr Gly 1045 1050 1055 1060 Asp Asp Met Val Thr Asp Gin Ala Phe Glu Asp Arg Leu Lys Glu Ala Glu Arg Glu Val 1065 1070 1075 1080 Thr Asp Leu Leu Arg Glu Ala Gin Glu Val Lys Asp Val Asp Gin Asn Leu Met Asp Arg 1085 1090 1095 1100 Leu Gin Arg Val Asn Ser Ser Leu His Ser Gin He Ser Arg Leu Gin Asn He Arg Asn 1105 1110 1115 1120 Thr He Glu Glu Thr Gly He Leu Ala Glu Arg Ala Arg Ser Arg Val Glu Ser Thr Glu 1125 1130 1135 1140 Gin Leu He Glu He Ala Ser Arg Glu Leu Glu Lys Ala Lys Met Ala Ala Ala Asn Val 1145 1150 1155 1160 Ser He Thr Gin Pro Glu Ser Thr Gly Glu Pro Asn Asn Met Thr Leu Leu Ala Glu Glu 1165 1170 1175 1180 Ala Arg Arg Leu Ala Glu Arg His Lys Gin Glu Ala Asp Asp He Val Arg Val Ala Lys 1185 1190 1195 1200 Thr Ala Asn Glu Thr Ser Ala Glu Ala Tyr Asn Leu Leu Leu Arg Thr Leu Ala Gly Glu 1205 1210 1215 1220 Asn Gin Thr Ala Leu Glu He Glu Glu Leu Asn Arg Lys Tyr Glu Gin Ala Lys Asn He 1225 1230 1235 1240 Ser Gin Asp Leu Glu Lys Gin Ala Ala Arg Val His Glu Glu Ala Lys Arg Ala Gly Asp 1245 1250 1255 1260 Lys Ala Val Glu He Tyr Ala Ser Val Ala Gin Leu Thr Pro Val Asp Ser Glu Ala Leu 1265 1270 1275 1280 Glu Asn Glu Ala Asn Lys He Lys Lys Glu Ala Ala Asp Leu Asp Arg Leu He Asp Gin 1285 1290 1295 1300 Lys Leu Lys Asp Tyr Glu Asp Leu Arg Glu Asp Met Arg Gly Lys Glu His Glu Val Lys 1305 1310 1315 1320 Asn Leu Leu Glu Lys Gly Lys Ala Glu Gin Gin Thr Ala Asp Gin Leu Leu Ala Arg Ala 1325 1330 1335 1340 Asp Ala Ala Lys Ala Leu Ala Glu Glu Ala Ala Lys Lys Gly Arg Ser Thr Leu Gin Glu 1345 1350 1355 1360 Ala Asn Asp He Leu Asn Asn Leu Lys Asp Phe Asp Arg Arg Val Asn Asp Asn Lys Thr 1365 1370 1375 1380 Ala Ala Glu Glu Ala Leu Arg Arg He Pro Ala He Asn Arg Thr He Ala Glu Ala Asn 1385 1390 1395 1400 Glu Lys Thr Arg Glu Ala Gin Leu Ala Leu Gly Asn Ala Ala Ala Asp Ala Thr Glu Ala 1405 1410 1415 1420 Lys Asn Lys Ala His Glu Ala Glu Arg He Ala Ser Ala Val Gin Lys Asn Ala Thr Ser 1425 1430 1435 1440 Thr Lys Ala Asp Ala Glu Arg Thr Phe Gly Glu Val Thr Asp Leu Asp Asn Glu Val Asn 1445 1450 1455 1460 Gly Met Leu Arg Gin Leu Glu Glu Ala Glu Asn Glu Leu Lys Arg Lys Gin Asp Asp Ala 1465 1470 1475 1480 Asp Gin Asp Met Met Met Ala Gly Met Ala Ser Gin Ala Ala Gin Glu Ala Glu Leu Asn 1485 1490 1495 1500 Ala Arg Lys Ala Lys Asn Ser Val Ser Ser Leu Leu Ser Gin Leu Asn Asn Leu Leu Asp 1505 1510 1515 1520 Gin Leu Gly Gin Leu Asp Thr Val Asp Leu Asn Lys Leu Asn Glu He Glu Gly Ser Leu 1525 1530 1535 1540 Asn Lys Ala Lys Asp Glu Met Lys Ala Ser Asp Leu Asp Arg Lys Val Ser Asp Leu Glu 1545 1550 1555 1560 Ser Glu Ala Arg Lys Gin Glu Ala Ala He Met Asp Tyr Asn Arg Asp He Ala Glu He 1565 1570 1575 1580 He Lys Asp He His Asn Leu Glu Asp He Lys Lys Thr Leu Pro Thr Gly Cys Phe Asn 1585 1590 1595 1600 Thr Pro Ser He Glu Lys Pro 1605 INFORMATION FOR SEQ ID NO: 11: SEQUENCE CHARACTERISTICS (A) LENGTH: 1609 AMINO ACIDS (B) TYPE: AMINO ACID (C) STRANDEDNESS: (D) TOPOLOGY: LINEAR (E) AMINO ACID NUMBERING ACCORDING TO TRANSLATION OF GENEBANK ACCESSION NUMBER PI1047; MOLECULAR TYPE: PROTEIN SEQUENCE DESCRIPTION: SEQ ID NO 11: Met Arg Gly Ser His Arg Ala Ala Pro Ala Leu Arg Pro Arg Gly Arg Leu Trp Pro Val 1 5 10 15 20 Leu Ala Val Leu Ala Ala Ala Ala Ala Ala Gly Cys Ala Gin Ala Ala Met Asp Glu Cys 25 30 35 40 Thr Asp Glu Gly Gly Arg Pro Gin Arg Cys Met Pro Glu Phe Val Asn Ala Ala Phe Asn 45 50 55 60 Val Thr Val Val Ala Thr Asn Thr Cys Gly Thr Pro Pro Glu Glu Tyr Cys Val Gin Thr 65 70 75 80 Gly Val Thr Gly Val Thr Lys Ser Cys His Leu Cys Asp Ala Gly Gin Pro His Leu Gin 85 90 95 100 His Gly Ala Ala Phe Leu Thr Asp Tyr Asn Asn Gin Ala Asp Thr Thr Trp Trp Gin Ser 105 110 115 120 Gin Thr Met Leu Ala Gly Val Gin Tyr Pro Ser Ser He Asn Leu Thr Leu His Leu Gly 125 130 135 140 Lys Ala Phe Asp He Thr Tyr Val Arg Leu Lys Phe His Thr Ser Arg Pro Glu Ser Phe 145 150 155 160 Ala He Tyr Lys Arg Thr Arg Glu Asp Gly Pro Trp He Pro Tyr Gin Tyr Tyr Ser Gly 165 170 175 180 Ser Cys Glu Asn Thr Tyr Ser Lys Ala Asn Arg Gly Phe He Arg Thr Gly Gly Asp Glu 185 190 195 200 Gin Gin Ala Leu Cys Thr Asp Glu Phe Ser Asp Phe Ser Pro Leu Thr Gly Gly Asn Val 205 210 215 220 Ala Phe Ser Thr Leu Glu Gly Arg Pro Ser Ala Tyr Asn Phe Asp Asn Ser Pro Val Leu 225 230 235 240 Gin Glu Trp Val Thr Ala Thr Asp He Arg Val Thr Leu Asn Arg Leu Asn Thr Phe Gly 245 250 255 260 Asp Glu Val Phe Asn Asp Pro Lys Val Leu Lys Ser Tyr Tyr Tyr Ala He Ser Asp Phe 265 270 275 280 Ala Val Gly Gly Arg Cys Lys Cys Asn Gly His Ala Ser Glu Cys Met Lys Asn Glu Phe 285 290 295 300 Asp Lys Leu Val Cys Asn Cys Lys His Asn Thr Tyr Gly Val Asp Cys Glu Lys Cys Leu 305 310 315 320 Pro Phe Phe Asn Asp Arg Pro Trp Arg Arg Ala Thr Ala Glu Ser Ala Ser Glu Cys Leu 325 330 335 340 Pro Cys Asp Cys Asn Gly Arg Ser Gin Glu Cys Tyr Phe Asp Pro Glu Leu Tyr Arg Ser 345 350 355 360 Thr Gly His Gly Gly His Cys Thr Asn Cys Gin Asp Asn Thr Asp Gly Ala His Cys Glu 365 370 375 380 Arg Cys Arg Glu Asn Phe Phe Arg Leu Gly Asn Asn Glu Ala Cys Ser Ser Cys His Cys 385 390 395 400 Ser Pro Val Gly Ser Leu Ser Thr Gin Cys Asp Ser Tyr Gly Arg Cys Ser Cys Lys Pro 405 410 415 420 Gly Val Met Gly Asp Lys Cys Asp Arg Cys Gin Pro Gly Phe His Ser Leu Thr Glu Ala 425 430 435 440 Gly Cys Arg Pro Cys Ser Cys Asp Pro Ser Gly Ser He Asp Glu Cys Asn Val Glu Thr 445 450 455 460 Gly Arg Cys Val Cys Lys Asp Asn Val Glu Gly Phe Asn Cys Glu Arg Cys Lys Pro Gly 465 470 475 480 Phe Phe Asn Leu Glu Ser Ser Asn Pro Arg Gly Cys Thr Pro Cys Phe Cys Phe Gly His 485 490 495 500 Ser Ser Val Cys Thr Asn Ala Val Gly Tyr Ser Val Tyr Ser He Ser Ser Thr Phe Gin 505 510 515 520 He Asp Glu Asp Gly Trp Arg Ala Glu Gin Arg Asp Gly Ser Glu Ala Ser Leu Glu Trp 525 530 535 540 Ser Ser Glu Arg Gin Asp He Ala Val He Ser Asp Ser Tyr Phe Pro Arg Tyr Phe He 545 550 555 560 Ala Pro Ala Lys Phe Leu Gly Lys Gin Val Leu Ser Tyr Gly Gin Asn Leu Ser Phe Ser 565 570 575 580 Phe Arg Val Asp Arg Arg Asp Thr Arg Leu Ser Ala Glu Asp Leu Val Leu Glu Gly Ala 585 590 595 600 Gly Leu Arg Val Ser Val Pro Leu He Ala Gin Gly Asn Ser Tyr Pro Ser Glu Thr Thr 605 610 615 620 Val Lys Tyr Val Phe Arg Leu His Glu Ala Thr Asp Tyr Pro Trp Arg Pro Ala Leu Thr 625 630 635 640 Pro Phe Glu Phe Gin Lys Leu Leu Asn Asn Leu Thr Ser He Lys He Arg Gly Thr Tyr 645 650 655 660 Ser Glu Arg Ser Ala Gly Tyr Leu Asp Asp Val Thr Leu Ala Ser Ala Arg Pro Gly Pro 665 670 675 680 Gly Val Pro Ala Thr Trp Val Glu Ser Cys Thr Cys Pro Val Gly Tyr Gly Gly Gin Phe 685 690 695 700 Cys Glu Met Cys Leu Ser Gly Tyr Arg Arg Glu Thr Pro Asn Leu Gly Pro Tyr Ser Pro 705 710 715 720 Cys Val Leu Cys Ala Cys Asn Gly His Ser Glu Thr Cys Asp Pro Glu Thr Gly Val Cys 725 730 735 740 Asn Cys Arg Asp Asn Thr Ala Gly Pro His Cys Glu Lys Cys Ser Asp Gly Tyr Tyr Gly 745 750 755 760 Asp Ser Thr Ala Gly Thr Ser Ser Asp Cys Gin Pro Cys Pro Cys Pro Gly Gly Ser Ser 765 770 775 780 Cys Ala Val Val Pro Lys Thr Lys Glu Val Val Cys Thr Asn Cys Pro Thr Gly Thr Thr 785 790 795 800 Gly Lys Arg Cys Glu Leu Cys Asp Asp Gly Tyr Phe Gly Asp Pro Leu Gly Arg Asn Gly 805 810 815 820 Pro Val Arg Leu Cys Arg Leu Cys Gin Cys Ser Asp Asn He Asp Pro Asn Ala Val Gly 825 830 835 840 Asn Cys Asn Arg Leu Thr Gly Glu Cys Leu Lys Cys He Tyr Asn Thr Ala Gly Phe Tyr 845 850 855 860 Cys Asp Arg Cys Lys Asp Gly Phe Phe Gly Asn Pro Leu Ala Pro Asn Pro Ala Asp Lys 865 870 875 880 Cys Lys Ala Cys Asn Cys Asn Pro Tyr Gly Thr Met Lys Gin Gin Ser Ser Cys Asn Pro 885 890 895 900 Val Thr Gly Gin Cys Glu Cys Leu Pro His Val Thr Gly Gin Asp Cys Gly Ala Cys Asp 905 910 915 920 Pro Gly Phe Tyr Asn Leu Gin Ser Gly Gin Gly Cys Glu Arg Cys Asp Cys His Ala Leu 925 930 935 940 Gly Ser Thr Asn Gly Gin Cys Asp He Arg Thr Gly Gin Cys Glu Cys Gin Pro Gly He 945 950 955 960 Thr Gly Gin His Cys Glu Arg Cys Glu Val Asn His Phe Gly Phe Gly Pro Glu Gly Cys 965 970 975 980 Lys Pro Cys Asp Cys His Pro Glu Gly Ser Leu Ser Leu Gin Cys Lys Asp Asp Gly Arg 985 990 995 1000 Cys Glu Cys Arg Glu Gly Phe Val Gly Asn Arg Cys Asp Gin Cys Glu Glu Asn Tyr Phe 1005 1010 1015 1020 Tyr Asn Arg Ser Trp Pro Gly Cys Gin Glu Cys Pro Ala Cys Tyr Arg Leu Val Lys Asp 1025 1030 1035 1040 Lys Val Ala Asp His Arg Val Lys Leu Gin Glu Leu Glu Ser Leu He Ala Asn Leu Gly 1045 1050 1055 1060 Thr Gly Asp Glu Met Val Thr Asp Gin Ala Phe Glu Asp Arg Leu Lys Glu Ala Glu Arg 1065 1070 1075 1080 Glu Val Met Asp Leu Leu Arg Glu Ala Gin Asp Val Lys Asp Val Asp Gin Asn Leu Met 1085 1090 1095 1100 Asp Arg Leu Gin Arg Val Asn Asn Thr Leu Ser Ser Gin He Ser Arg Leu Gin Asn He 1105 1110 1115 1120 Arg Asn Thr He Glu Glu Thr Gly Asn Leu Ala Glu Gin Ala Arg Ala His Val Glu Asn 1125 1130 1135 1140 Thr Glu Arg Leu He Glu He Ala Ser Arg Glu Leu Glu Lys Ala Lys Val Ala Ala Ala 1145 1150 1155 1160 Asn Val Ser Val Thr Gin Pro Glu Ser Thr Gly Asp Pro Asn Asn Met Thr Leu Leu Ala 1165 1170 1175 1180 Glu Glu Ala Arg Lys Leu Ala Glu Arg His Lys Gin Glu Ala Asp Asp He Val Arg Val 1185 1190 1195 1200 Ala Lys Thr Ala Asn Asp Thr Ser Thr Glu Ala Tyr Asn Leu Leu Leu Arg Thr Leu Ala 1205 1210 1215 1220 Gly Glu Asn Gin Thr Ala Phe Glu He Glu Glu Leu Asn Arg Lys Tyr Glu Gin Ala Lys 1225 1230 1235 1240 Asn He Ser Gin Asp Leu Glu Lys Gin Ala Ala Arg Val His Glu Glu Ala Lys Arg Ala 1245 1250 1255 1260 Gly Asp Lys Ala Val Glu He Tyr Ala Ser Val Ala Gin Leu Ser Pro Leu Asp Ser Glu 1265 1270 1275 1280 Thr Leu Glu Asn Glu Ala Asn Asn He Lys Met Glu Ala Glu Asn Leu Glu Gin Leu He 1285 1290 1295 1300 Asp Gin Lys Leu Lys Asp Tyr Glu Asp Leu Arg Glu Asp Met Arg Gly Lys Glu Leu Glu 1305 1310 1315 1320 Val Lys Asn Leu Leu Glu Lys Gly Lys Thr Glu Gin Gin Thr Ala Asp Gin Leu Leu Ala 1325 1330 1335 1340 Arg Ala Asp Ala Ala Lys Ala Leu Ala Glu Glu Ala Ala Lys Lys Gly Arg Asp Thr Leu 1345 1350 1355 1360 Gin Glu Ala Asn Asp He Leu Asn Asn Leu Lys Asp Phe Asp Arg Arg Val Asn Asp Asn 1365 1370 1375 1380 Lys Thr Ala Ala Glu Glu Ala Leu Arg Lys He Pro Ala He Asn Gin Thr He Thr Glu 1385 1390 1395 1400 Ala Asn Glu Lys Thr Arg Glu Ala Gin Gin Ala Leu Gly Ser Ala Ala Ala Asp Ala Thr 1405 1410 1415 1420 Glu Ala Lys Asn Lys Ala His Glu Ala Glu Arg He Ala Ser Ala Val Gin Lys Asn Ala 1425 1430 1435 1440 Thr Ser Thr Lys Ala Glu Ala Glu Arg Thr Phe Ala Glu Val Thr Asp Leu Asp Asn Glu 1445 1450 1455 1460 Val Asn Asn Met Leu Lys Gin Leu Gin Glu Ala Glu Lys Glu Leu Lys Arg Lys Gin Asp 1465 1470 1475 1480 Asp Ala Asp Gin Asp Met Met Met Ala Gly Met Ala Ser Gin Ala Ala Gin Glu Ala Glu 1485 1490 1495 1500 He Asn Ala Arg Lys Ala Lys Asn Ser Val Thr Ser Leu Leu Ser He He Asn Asp Leu 1505 1510 1515 1520 Leu Glu Gin Leu Gly Gin Leu Asp Thr Val Asp Leu Asn Lys Leu Asn Glu He Glu Gly 1525 1530 1535 1540 Thr Leu Asn Lys Ala Lys Asp Glu Met Lys Val Ser Asp Leu Asp Arg Lys Val Ser Asp 1545 1550 1555 1560 Leu Glu Asn Glu Ala Lys Lys Gin Glu Ala Ala He Met Asp Tyr Asn Arg Asp He Glu 1565 1570 1575 1580 Glu He Met Lys Asp He Arg Asn Leu Glu Asp He Arg Lys Thr Leu Pro Ser Gly Cys 1585 1590 1595 1600 Phe Asn Thr Pro Ser He Glu Lys Pro 1605

Claims: CLAIMS We claim: 1. A method for treating an amyloid disease in a patient, the method comprising administrating to the patient a therapeutically effective amount of a polypeptide having a conformational similarity to a fragment of a laminin protein. 2. The method of claim 1 wherein the conformational similarity is at least 70%. 3. The method of claim 1 wherein the conformational similarity is at least 90%. 4. The method of claim 1 wherein the polypeptide is synthesized to achieve said conformational similarity. 5. The method of claim 1 wherein said amyloid disease is Alzheimer's disease. 6. The method of claim 1 wherein said fragment is intact laminin. 7. The method of claim 1 wherein the laminin fragment is a laminin A chain. 8. The method of claim 7 wherein the laminin A chain is derived from mammals. 9. The method of claim 8 wherein the fragment comprises a polypeptide as set forth in SEQ ID NO: 5 or a fragment thereof. 10. The method of claim 8 wherein the fragment comprises a polypeptide as set forth in SEQ ID NO: 4 or a fragment thereof. 11. The method of claim 1 wherein the laminin fragment includes a globular domain repeat within the laminin A chain or a fragment thereof. 12. The method of claim 11 wherein the globular repeats include the peptide sequence of SEQ ID NO: 3 or a fragment thereof. 13. The method of claim 11 wherein the globular repeats include the peptide sequence of SEQ ID NO: 2 or a fragment thereof. 14. The method of claim 11 wherein the laminin fragment includes the peptide sequence of SEQ ID NO: 1 or a fragment thereof. 15. A method for the treatment of a patient having an identified clinical need to interfere with the pathological effects of amyloid, the method comprising: administering to the patient a therapeutically effective amount of a polypeptide selected from the group consisting of human laminin, mouse laminin, SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO 4:, SEQ ID NO: 5, SEQ ID NO:6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, and fragments thereof. 16. A method to diagnose a disease or a susceptibility to a disease related to the levels of laminin or laminin-derived protein fragments, the method comprising determining levels of laminin or a particular laminin-derived protein fragment in a sample, whereby the levels are indicative of the presence of a disease, susceptibility to a disease, or progression of said disease. 17. The method of claim 16 wherein said disease is an amyloid disease. 18. The method of claim 16 wherein said laminin or laminin-derived protein fragments is selected from the group consisting of human laminin, mouse laminin, SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO 4:, SEQ ID NO: 5, SEQ ID NO:6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO:10, SEQ ID NO: 11, and fragments thereof. 19. The method of claim 16 wherein said laminin-derived protein fragment is a 130 kilodalton fragment detected by ligand blotting with biotinylated beta-amyloid protein (AI3), and quantitated by scanning densitometry or by ELISA. 20. The method of claim 16 wherein the sample assayed is a biological fluid. 21. The method of claim 20 wherein the biological fluid is serum. 22. The method of claim 20 wherein the biological fluid is derived from humans. 23. A method of making an antibody, the method comprising producing antibodies from a peptide sequence within the 130 kilodalton AB-laminin binding fragment present in human biological fluids. I l l 24. The method of claim 23 wherein antibody production comprises production of at least one type of antibody selected from the group consisting of polyclonal, monoclonal, chimeric antibodies, and anti-idiotypic antibodies. 25. The method of claim 23 wherein the peptide sequence is selected from the group of SEQ ID s consisting of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO 4:, SEQ ID NO: 5, SEQ ID NO:6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, and fragments thereof. 26. The method of claim 23 further comprising monitoring a biological fluid for the presence and extent of laminin and laminin-derived protein fragments as an indicator for the extent of an amyloid disease. 27. A process for diagnosing a disease or a susceptibility to a disease related to an underexpression or overexpression of a polypeptide, comprising determining a mutation in a nucleic acid sequence encoding a polypeptide selected from the group consisting of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO 4:, SEQ ID NO: 5, SEQ ID NO:6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO:10, SEQ ID NO: 11, and fragments thereof. 28. The method of claim 23 further comprising radiolabelling the antibodies for radioimaging or in vivo diagnosis for detection of laminin and laminin-derived protein fragments. 29. A method for detection and quantification of laminin and laminin-derived fragments in biological fluids comprising a) allowing a first laminin or laminin-derived fragment antibody to bind to microtiter wells for a sufficient time to allow said binding, b) adding a quantity of biological fluid to the microtiter wells, c) incubating the biological fluid for sufficient time to allow binding of any laminin or laminin-derived fragment in the biological fluid to the first antibody on the microtiter wells, d) adding a second labeled antibody to the microtiter wells wherein the second labelled antibody is against the laminin or laminin-derived fragment, but which is against a different epitope than the first antibody, and allowing the second antibody to bind to any laminin or laminin-derived fragment captured by the first antibody, and e) detecting bound materials using an appropriate substrate or label. 30. A composition of matter comprising a purified laminin polypeptide fragment that is capable of binding to Aβ amyloid protein, wherein the laminin polypeptide fragment has an Aβ binding site within a globular repeating domain of laminin A chain. 31. The laminin polypeptide fragment of claim 30 wherein the fragment comprises a 55 kilodalton elastase-resistent laminin polypeptide fragment. 32. The laminin polypeptide fragment of claim 31 wherein the fragment comprises a 55 kilodalton laminin polypeptide fragment that is produced using a protease from the group of proteases consisting of trypsin and elastase. 33. The laminin polypeptide fragment of claim 32 wherein the fragment comprises SEQ ID NO: 5. 34. A method of in vivo inhibition of AB amyloidosis comprising: a) introducing a vector comprising the DNA sequence encoding a laminin polypeptide fragment that is capable of binding to AJ3 amyloid protein, wherein the laminin polypeptide fragment has an AB binding site within a globular repeating domain of laminin A chain, b) producing said laminin polypeptide fragment in vivo to inhibit AB amyloidosis. 35. A method of in vivo inhibition of AB amyloidosis comprising: a) introducing a vector comprising the DNA sequence encoding the polypeptide of SEQ ID NO: 3 or a fragment thereof, b) producing a peptide fragment having the polypeptide sequence of SEQ ID NO: 3 in vivo to inhibit AB amyloidosis. 36. The method of claim 1 wherein the fragment of laminin protein is an amyloid binding fragment of laminin protein

Inventors: CASTILLO GERARDO, SNOW ALAN D, CASTILLO, GERARDO, SNOW, ALAN, D.
Applicants: UNIV WASHINGTON, UNIVERSITY OF WASHINGTON
Application year: 1997
Main classification: A01N37
IPC codes: A61K38, C07K14