bluuebunny/crossref_metadata_2025_split huggingface dataset:
The Antigenic Properties of Extracts of Horse Dander
Authors: Longcope W. T. , O'Brien D. P. , Perlzweig W. A. 
Published: December 2022

Abstract
In a previous communication (1) it was shown that extracts of horse dander contain an antigen, or antigens, that are capable of sensitizing guinea pigs. This can be brought about quite readily, so that guinea pigs sensitized by one or two intraperitoneal injections of the extract, die in typical anaphylactic shock when, at least three weeks later, comparatively small amounts of the extract are injected intravenously. Sensitization can also be demonstrated by employing the uterine muscle strip. The extract likewise acts as a specific antigen, for guinea pigs sensitized to it do not react to horse serum, or to the extracts of dander of dogs and cats; nor do guinea pigs sensitized to horse serum react to extracts of horse dander. The present studies were made with the object of investigating the nature of the antigen or antigens contained in these extracts.
Regulation of Antibody Response in Vitro
Authors: Kishimoto Tadamitsu , Ishizaka Kimishige 
Published: December 2022

Abstract
Rabbits were primed with Ascaris antigen (Asc) included in either aluminum hydroxide gel (alum) or in complete Freund's adjuvant (CFA), followed by immunization with DNP-coupled Asc (DNP-Asc) in alum at 4 weeks. Effect of priming with free carrier on the development of DNP-specific (B)2 memory cells was analyzed by measuring in vitro antihapten antibody response of their mesenteric lymph node cells to DNP-Asc. The lymph node cells obtained from these animals responded to the antigen in a similar manner as the cells obtained from the animals which were immunized by two 4-weeks-apart injections of DNP-Asc, with respect to: 1) the class distribution of the antibodies between IgG and IgM; and 2) the optimal antigen concentration required for maximal antibody response. These cells formed more IgG antibody than IgM antibody, whereas the lymph node cells obtained after a primary immunization with DNP-Asc formed more IgM than IgG antibody. The optimal antigen concentration required for maximal antibody formation became less when the donors were preimmunized with free carrier, indicating that carrier-specific helper cells may have involved in emergence or selective proliferation of hapten-specific memory cells bearing high affinity receptor. Priming with free Asc in alum showed the carrier effect on the anti-DNP IgE antibody formation, whereas priming with the same antigen in CFA did not. Mesenteric lymph node cells obtained from the alum group formed anti-DNP IgE antibody but the cells from the CFA group failed to do so. No significant difference was observed between the CFA group and alum group with respect to the anti-Asc and anti-DNP IgG antibody titer or to the ability of their lymph node cells to form the IgG antibodies in vitro. The findings indicated that the difference between the two groups in the IgE antibody response is due to some difference in the carrier-specific (T) cell population. The results suggest that carrier-specific (T) helper cells regulate the class distribution and affinity of antihapten antibodies through the exertion of some selective pressure on the generation of hapten-specific (B) memory cells.
Morphologic, Chemical, and Immunologic Studies of Amyloid-Like Fibrils Formed from Bence Jones Proteins by Proteolysis
Authors: Linke R. P. , Zucker-Franklin D. , Franklin E. C. 
Published: December 2022

Abstract
Seventy-five Bence Jones Proteins (BJP) were digested with pepsin. Forty-six of 61 λ and 9 of 14 k-BJP formed precipitates but only 10 of them (9 λ and 1 κ) showed strong congo red uptake, green polarization birefringence, and dichroism. Electron microscopic studies revealed fibrils in eight of which three resembled isolated human amyloid fibrils and five had fibrils atypical for amyloid. Digestion of one BJP with different enzymes resulted in amyloid-like fibrils having different morphologic appearances.
One VλI Oz(-) BJP (CAR) was investigated more intensively. Its peptic digest consisted of 70% of an 8000 dalton fragment and 30% of a 12,000 m.w. fragment which were able to form amyloid-like fibrils even after purification. Both appeared to be derived from the variable region by peptide maps. The amino acid sequence of the first 10 residues of the 8000 m.w. fragment placed it in the V region commencing with residue 5.
Tryptic digestion yielded a 13,000 m.w. preamyloid fragment which remained soluble at neutral pH and thus proved suitable for immunologic studies. Studies with antisera to native BJP CAR, the tryptic preamyloid and oxidized BJP CAR indicated that the preamyloid contained idiotypic variable region antigenic determinants which could be revealed either by oxidation or proteolytic digestion of the native precursor BJP. These findings may help to explain the failure of most antisera to native L-chains to react with naturally occurring amyloid proteins.
Genetic Control of Immune Response toward the Loop Region of Lysozyme
Authors: Maron Elchanan , Scher Howard I. , Mozes Edna , Arnon Ruth , Sela Michael 
Published: December 2022

Abstract
Analysis of the immune response toward the lysozyme “loop” region attached to multichain poly-dl-alanine (loop-A-L) in DBA/1 (high responder) and SJL (low responder) mouse strains, as well as in their F1 hybrids and backcrosses, showed that the antibody production to loop is genetically controlled by a unigenic dominant trait, which is not linked to the major histocompatibility locus H-2.
The strain-dependent differences, in the response to the loop, observed previously upon immunization with loop-A—L, were now confirmed with the loop-Pro—L (loop attached to multichain polyproline) conjugate, with the exception of the SWR mice—high responders to loop-A-L and low responders to loop-Pro-L—which were also found incapable of responding to the Pro-L carrier.
Immunization of several inbred mouse strains with conjugates of a synthetic loop derivative yielded similar strain-dependent differences to those obtained with the conjugates of the natural lysozyme loop.
The Role of Antigenic Determinants in the Control of IgM and IgG Antibody Responses to Denatured DNA
Authors: Gruenewald Ruben , Stollar B. David 
Published: December 2022

Abstract
Rabbits immunized with complexes of denatured calf thymus DNA and methylated bovine serum albumin (MBSA) produced only IgM antibodies to denatured DNA, confirming the results of previous studies. In contrast, both IgM and IgG antibodies were induced by MBSA complexes of T4 and T6 bacteriophage DNA, in which the normal base cytosine is replaced by glucosylated hydroxymethylcytosine. The glucose in not essential for this switch, since a preparation of modified T2 phage DNA, which contained nonglucosylated hydroxymethylcytosine, also induced the formation of both classes of antibodies. With or without glycosylation, the hydroxymethylcytosine served as a dominating determinant for specificity as well as a signal for 7S antibody production. The validity of complement fixation as an assay for these responses was confirmed by quantitative precipitation tests.
Intracellular Localization of Mammalian Type C Virus Species-Specific (gs-1) and Interspecies-Specific (gs-3) Antigenic Determinants with the Indirect Immunoperoxidase Technique and Light Microscopy
Authors: Girardi Anthony , Hampar Berge , Hsu Konrad C. , Oroszlan Stephan , Hornberger Elizabeth , Kelloff Gary , Gilden Raymond V. 
Published: December 2022

Abstract
The indirect immunoperoxidase staining technique was used for localizing by light microscopy the intracellular species-specific and interspecies-specific antigenic determinants of a panel of murine and hamster type C viruses, and was compared to the immunofluorescent technique. The antisera were prepared against antigens purified by isoelectric focusing and also were obtained from MSV tumor-bearing rats. The results indicate that the immunoperoxidase technique is suitable for detecting antigens associated with mammalian type C viruses, and appears to be more sensitive than the immunofluorescent procedure without sacrificing specificity.
Complement: a Reversible Temperature-Dependent Alteration in the Reactivity of EAC1 with C4
Authors: Linscott William D. 
Published: December 2022

Abstract
Conditions which favored the production of hemolytically competent C4 sites over incompetent C4 sites on IgM-sensitized cells included a low ratio of Ab:C1 (SA:SAC1 ratio), prior exposure of the EAC1 to 0°C for 30 min or more, and reactive with C4 at 0°C. Other important factors included Ab class, C1 and C4 multiplicity, and the time of incubation. The status of a given C4 site seemed to be set irrevocably at the time C4 first interacted with SAC1, and this status was associated with the affinity with which the C1 was bound to the cell. Cell-bound C1 underwent a completely reversible “super-activation” at 0°C which increased the proportion of hemolytically competent C4 sites generated during subsequent interaction with C4. The configuration of a C1 molecule, as determined by the affinity with which it is bound to a cell, may determine the hemolytic competence of a C4 molecule reacting with that site.
Water Buffalo Blood Groups. IV. Antigenic Determinant Located beneath the Surface of Red Cells
Authors: Iannelli D. , Bettini T. M. , Oreste U. 
Published: December 2022

Summary
In water buffalo, two paternal half-sibs have been identified which, when used as recipients, produced antibodies of the same specificity as those they stimulated when used as donors. The apparent serologic paradox is presumably due to an antigenic determinant located beneath the surface of erythrocytes.
Protection of Adult Mice against Tumor Challenge by Immunization with Irradiated Adult Skin or Embryo Cells
Authors: Bendich Aaron , Borenfreund Ellen , Stonehill Elliott H. 
Published: December 2022

Abstract
Water-soluble mouse embryo antigens, not detectable in normal adult visceral tissues, were found in each of 99 different cancerous tissues in 21 mouse strains (1, 2). Rabbit antiserum against the embryo constituents, absorbed with extracts of adult mouse internal organs, served as the diagnostic reagent in the agar double-diffusion precipitin tests which were employed for detection. Positive reactions were obtained not only with extracts of embryos and all cancers examined, but with extracts of the skin of adult animals as well.
Chromatographic estimation of the molecular weights of the antigens from embryos and tumors (65,000 to 70,000) revealed them to be about five times larger than the cross-reacting components in adult skin (10,000 to 15,000). The skin antigens were not detected in embryo viscera or in tumors, even in a sensitive radial immunodiffusion assay with the above antiserum (manuscript in preparation).
Physical and Chemical Studies on Human Properdin Purified by Elution from Zymosan and by Affinity Chromatography
Authors: Minta Joe O. , Lepow Irwin H. 
Published: December 2022

Abstract
Properdin purified to homogeneity from human serum after adsorption to and elution from zymosan (J. Immunol., 100: 142, 1968) is a glycoprotein containing about 9.8% carbohydrate. Preliminary analyses indicate 3.8% hexose, 1.5% hexosamine, 3.8% sialic acid, and 0.7% fucose. The V̄ calculated from amino acid composition and corrected for carbohydrate content was 0.70. Approach to equilibrium ultracentrifugation then yielded a molecular weight (m.w.)1 of 184,000 ± 12,000. In 6 M guanidine hydrochloride, properdin eluted from a 4% agarose column as a single protein peak with an estimated m.w. of 45,000, suggesting dissociation into four non-covalently linked subunits of similar or identical m.w. Since the possibility exists that zymosan-purified properdin may be in an altered state, properdin has been isolated by affinity chromatography. A column was charged with the IgG fraction of monospecific rabbit anti-human properdin which had been coupled to CNBr-activated Sepharose 4B (1:50 w/w) in 0.06 M barbital buffer, pH 9.6.
The C3 Feedback Cycle of C Activation: The Role of the C3b Inactivator (KAF)
Authors: Lachmann P. J. , Nicol P. A. E. 
Published: December 2022

Abstract
The immunochemical depletion of KAF from serum has been brought about by using purified F(ab')2 anti-KAF. The depleted serum undergoes a spontaneous activation of its alternate pathway, converting its GBG and depleting the co-factors required to form the “cobra venom C3 convertase.” All C3 becomes converted to C3b and if red cells are present C3 becomes fixed to them. This situation exactly parallels that seen in vivo in the unique KAF-deficient patient. The mechanism by which KAF depletion leads to activation of the alternate pathway has been shown to lie in its failure to activate C3b, since if C3 is first depleted from serum with F(ab')2 anti-C3 subsequent KAF depletion produces no alternate pathway activation. In serum depleted of C3 it is similarly found that neither zymosan, endotoxin nor inulin can induce the formation of a C3 convertase. It is therefore clear that the alternate pathway is in reality a C3-feedback pathway.
Isolation of Human C4 by Affinity Chromatography with IgG-Coupled Sepharose 6B
Authors: Patrick R. A. , Mernitz Janice , Bing D. H. 
Published: December 2022

Abstract
At least four examples exist which demonstrate an association of C4 with serum proteins. It has been previously reported that C4 forms association products with itself and with human 7S γ-globulin in the presence of C1s̄. Native C4 is known to complex with C2 in a reversible fashion. This reversible association of C2 and C4 is converted to a firm complex which is due to the proteolytic action of C1s̄. Finally, C4 is believed to react with receptor sites on antibody molecules as well as erythrocyte membrane receptors during immune hemolysis.
Human IgG was covalently linked to Sepharose 6B under basic conditions by use of cyanogen bromide. The resultant Sepharosecoupled IgG was stored at 4°C with 0.005% sodium azide until ready for use. Approximately 1 mg of IgG was bound per 20 mg Sepharose. Crude C4 from a pseudoglobulin fraction of human serum and subsequently eluted from DEAE-cellulose at pH 7.3 was used for studies with insoluble IgG.
Hereditary C6 Deficiency in Man
Authors: Leddy J. P. , Frank M. M. , Gaither T. , Heusinkveld R. S. , Breckenridge R. T. , Klemperer M. R. 
Published: December 2022

Abstract
An 18-year-old black female (D.B.) in good general health was found to have no hemolytic activity in repeated serum CH50 titrations. Functional assays yielded normal values for all C components except C6. C6 was not detectable a) by functional assays utilizing either stepwise buildup of C components on EA or reconstitution of C6-deficient rabbit serum, or b) by immunodiffusion against antiserum to rabbit C6. Hemolytic activity was restored by addition of functionally pure C6. Hemolytic C (CH50) titers on family members were normal. By specific functional assay, however, both parents and five of six available siblings had approximately half-normal serum C6 levels. The other sibling was normal. C6 deficiency in the proband could not be accounted for by a serum inhibitor; C6 was also absent in D.B. plasma. Biologic properties of D.B. serum include: a) absent bactericidal activity against Salmonella typhi 0 901 with or without added rabbit antibody; b) normal generation of chemotactic activity for human neutrophils in the presence of endotoxin or aggregated IgG; c) ability to sensitize appropriate cells for immune adherence or agglutination by anti-C3 Coombs serum; and d) inability to lyse PNH red cells in either acid hemolysis or “sugar water” tests.
The Chemotactic Factor Inactivator in Normal Human Serum
Authors: Till G. , Ward P. A. 
Published: December 2022

Abstract
Normal human serum contains a chemotactic factor inactivator (CFI) that irreversibly inhibits the neutrophil chemotactic activity associated with fragments of C3 and C5, the C complex, and the bacterial chemotactic factor derived from Escherichia coli. Physicochemical features of CFI include the following: it is present in the pseudoglobulin fraction of serum, soluble in ammonium sulfate at 60% saturation, and elutes in at least two different zones in ion exchange chromatography and in Sephadex gel filtration. Electrophoretically CFI appears in positions of α- and β-globulins. CFI reacts in an enzymatic-like manner: the inactivation of chemotactic activity is progressive with time, is temperature-dependent, and is maximal at pH 7.3. CFI is heat labile, being destroyed at 56°C after ½ hr. Its activity is not blocked by 0.02 M EDTA, 0.02 M phenanthroline, soybean trypsin inhibitor, DFP or ε-aminocaproic acid. Caseinolytic activity and carboxypeptidase-B-like activity (measured by hydrolysis of hippuryl-l-arginine) are lacking in CFI preparations.
Receptors for Bound C3 on Neutrophil Membrane Fragments
Authors: Henson Peter M. 
Published: December 2022

Abstract
Neutrophils from rabbit and man have the property of adhering to particles (e.g., erythrocytes or zymosan) to which C3 is bound. Phagocytosis and release of granule constituents may follow. To study the receptors involved, we obtained plasma membrane fragments from these cells. A purified population of neutrophils was trace labeled with 125I anti-neutrophil antibody, disrupted in sucrose, and the nuclear debris, granules and soluble proteins were separated from the plasma membranes on sucrose gradients. Membrane fragments were labeled with 125I with lactoperoxidase and H2O2 and washed with saline. The fragments were examined by electron microscopy. Labeled membrane fragments from rabbit and human neutrophils were incubated with erythrocytes or zymosan, previously coated with C, which were then washed and counted. The fragments bound to EAC1423 but not to EAC142. Control preparations of rabbit erythrocyte membranes did not bind to EAC1423. The binding was partly temperature dependent and that of rabbit neutrophil membranes was inhibited by EDTA.
Isolation of the Seventh Component of the C System from Human Serum
Authors: Arroyave Carlos M. , Müller-Eberhard Hans J. 
Published: December 2022

Abstract
Isolation of C7 from human serum was carried out by a combination of Bio-Rex 70, DEAE-32, DEAE and CM 32 chromatography and preparative Pevikon block electrophoresis. The yield in terms of hemolytic activity was 0.5 to 1.5%. Purification was 1030-fold. The isolation and radiolabeled protein was identified by disc electrophoresis as a single protein and the C7 hemolytic activity could be localized to the position of this band. By two different methods the m.w. was determined to be 120,000. By immunoelectrophoresis the protein was found to be a slowly migrating β-globulin. The concentration in whole human serum was quantitated by the Mancini method to be 47 to 61 µg/ml. The efficiency of binding to sensitized sheep erythrocytes was found to be 5- to 10-fold greater when the protein was offered to EAC1-3 cells in presence of C5 and C6, rather than to EAC1-6 cells alone. Complete proportionality was obtained between -ln(1-y) and the dose of C7 protein employed.
The Terminal Components of the Nurse Shark (Ginglymostoma cirratum) C System
Authors: Jensen Joerg A. , Fuller Laphalle , Iglesias Elena 
Published: December 2022

Abstract
The preterminal (t1) and terminal (t2) C-components were isolated from nurse shark serum in functionally pure form. Preparative procedures included: a) low ionic strength precipitation (µ = 0.006, pH 7.6) where the activities stayed in the supernatant; b) DE-52; c) hydroxyapatite column chromatography; and d) gel filtration (G-200). In step (b) t1 eluted before t2 (µ = 0.006 and 0.06 at pH 7.6, respectively). In step (c) the order was reversed, t2 eluted with 0.2 M PO4, t1 with 0.5 M PO4 at pH 6.8. Functional purity was obtained after step (c). On a calibrated Sephadex G-200 column both components eluted with an IgG marker. The m.w. of t2 was determined by polyacrylamide gel electrophoresis; it was 185,000.
Both components were assayed hemolytically in two systems: 1) with a stable intermediate complex consisting of sheep E optimally sensitized with natural shark antibody and reacted sequentially with purified C1n and two shark serum fractions containing at least two still undefined C-components; and 2) with EAC1gpC4-C7hu.
Cerebrospinal Fluid C
Authors: Propp Richard P. 
Published: December 2022

Abstract
Determination of C3 concentration in unconcentrated cerebrospinal fluid by electroimmunodiffusion was possible only when an immunofixation layer was added by using antibody to the original gel antibody against C3. Recently we have been able to measure C4 in this manner, but in this situation the original running time is critical and must not be excessive since then the precipitate dissolves. This technique was applied to the study of paired sera and cerebrospinal fluids. Native C3 and C3 conversion products may be visualized by antigen-antibody crossed electrophoresis after concentration of cerebrospinal fluid 40-fold by ultrafiltration, providing the immunofixation procedure is used.
Ten normal specimens of cerebrospinal fluid had a mean (± 1 S.D.) of 378 ± 159 µg/100 ml for C3, with a mean C3/albumin of 1.49 ± 0.18%. Eight normal spinal fluids had a mean for C4 of 274, with a mean C4/albumin of 1.23%.
Initiation of Oxidative Metabolism in Human Neutrophils (PMN) by C Activated through an Alternate Pathway
Authors: Strauss Ronald G. , Mauer Alvin M. , Spitzer Roger E. , Asbrock Theresa , Stitzel Ann E. 
Published: December 2022

Abstract
An oxidative metabolic burst comparable to that after phagocytosis was initiated in normal PMN by exposing them to sera incubated with powdered inulin. In these sera a change in the electrophoretic mobility of the C3PA from beta to gamma indicated activation of the alternate pathway, while consumption of C3 indicated C activation. An increase of hexose monophosphate shunt activity in PMN greater than 5-fold indicated stimulation. Increases in O2 consumption, NBT dye reduction, and degranulation confirmed the metabolic burst. PMN metabolism was stimulated by inulin in fresh sera and in sera depleted of C4 from patients with active hereditary angioneurotic edema. Stimulation did not occur in the absence of serum, in sera heated to 50°C or 56°C for 30 min, in 0.02 M EDTA serum, in sera depleted of C3 or C3PA by adsorption at equivalence with monospecific antisera. The chemotactic response of these stimulated PMN was defective, suggesting altered membrane function.
Lysosomal Enzyme Release from Human Leukocytes: Mediation by the Alternate Pathway of Complement Activation
Authors: Goldstein Ira M. , Brai Melchiorre , Osler Abraham G. , Weissmann Gerald 
Published: December 2022

Abstract
The alternate pathway of complement activation has recently assumed an important role in the mediation of inflammation and tissue injury. We have found that complement activated via this pathway interacts with human polymorphonuclear leukocytes (PMN) in the absence of particulates and stimulates the selective release of lysosomal enzymes. Fresh human serum, after treatment with zymosan or cobra venom factor, yields a fluid phase component which induces cytochalasin B-treated PMN to release β-glucuronidase without leakage of cytoplasmic lactate dehydrogenase. Involvement of the alternate pathway of complement activation is evidenced by failure of serum to yield enzyme-releasing activity after pretreatment with rabbit antihuman C3 proactivator, 0.01 M EDTA but not 0.01 M EDTA, 0.02 M salicylaldoxime, 0.02 M hydrazine or by heating to 56°C for 30 min. Levels of C3 proactivator in treated sera correlated inversely with and perturbs the PMN plasma membrane sufficiently to cause lysosomal membrane perturbation, fusion, and ultimately lysosomal enzyme extrusion by a process of “reverse endocytosis.”