bluuebunny/crossref_metadata_2025_split huggingface dataset:
C3 Inactivator of Man
Authors: Ruddy Shaun , Austen K. Frank 
Published: December 2022

Summary
C3 Inactivator (C3INA) purified from human serum has been measured by its ability to block the reactivity of the cellular intermediate EAC143 in immune hemolysis. Cells prepared with limited amounts of C3 are reacted with C3INA, resulting in the inactivation of a portion of this cell-bound C3. The residual active cell-bound C3 is then detected by a stoichiometric assay in which the remaining components are supplied in relative excess. The average number of SAC143 inactivated by C3INA is a function of C3INA input. The inactivation of cell-bound C3 by C3INA is time and temperature dependent, and the rate of the inactivation is related to the input of C3INA. During the inactivation of SAC143 by C3INA, C3b or a fragment thereof is released into the fluid phase. C3INA is not consumed during its interaction with cell-bound C3 suggesting that it is an enzyme. Human C3INA appears to be identical to the conglutinogen-activating factor described by Lachmann and Müller-Eberhard.
Identification and Genetic Control of Three Rabbit γA Immunoglobulin Allotypes
Authors: Conway Thomas P. , Dray Sheldon , Lichter Edward A. 
Published: December 2022

Summary
Cross-immunization of rabbits with purified colostral γA immunoglobulin resulted in the production of three precipitating alloantibodies, which identified three γA immunoglobulin allotypes designated f1, f2 and f3. That these alloantibodies are specific for γA immunoglobulin was indicated by the similar precipitin arcs observed on immunoelectrophoresis when anti-f1, anti-f2 anti-f3, and goat anti-γA reacted with serum, whey or a highly purified colostral γA fraction. By immunoelectrophoresis with heterologous multispecific antisera to rabbit whey or serum and by ultracentrifugal analysis (s020,w = 10.9), the isolated γA appeared to be free of other serum proteins. By immunoelectrophoresis with anti-a and anti-b allotype antisera, the isolated γA immunoglobulins were also shown to possess heavy chain a locus and light chain b locus allotypic specificities. Allotype analysis of 521 progeny from eight mating combinations indicated that the allotypes f1, f2, and f3 are controlled by three allelic genes. This γA locus, designated f, was not closely linked to the X chromosome, the a or b immunoglobulin loci, the z α2 macroglobulin locus, the h haptoglobin locus or the q lipoprotein locus. Thus, in addition to the previously described unlinked a and b loci which are known to control allotypic specificities on the heavy and light chains of γA immunoglobulins, a third unlinked f locus is also involved in the control of serum and secretory γA immunoglobulins. This f locus, unlike the a and b loci, does not appear to be involved in the control of γG and γM immunoglobulins.
Prevention of Death from Endotoxin with Antisera:
Authors: Davis Charles E. , Brown Kenneth R. , Douglas Herndon , Tate William J. , Braude Abraham I. 
Published: December 2022

Summary
Rabbit antiserum against the endotoxins in smooth and rough bacteria, as well as rabbit antiserum against the endotoxins in heterologous organisms, prevented death in mice given lethal intravenous doses of endotoxin. These results indicated that different Gram-negative bacterial species share a protective antigen unrelated to “O” antigen. Similar protection was then attempted in mice with antisera prepared in the same animal family, i.e., rats. Instead of protecting, such sera sensitized mice so that otherwise sublethal doses of intravenous homologous endotoxin produced deaths from anaphylaxis within 1 hr. These small doses of endotoxin did not produce anaphylactic deaths in mice given immune rat serum prepared against unrelated (heterologous) endotoxins. The differential effects of protective rabbit antibody and anaphylactic rat antibody are thus attributed to reactions with different antigenic sites on the endotoxin molecule: anaphylactic antibody with the oligosaccharide “O” determinants, and protective antibody with a core antigen. Solution of the anaphylaxis problem is essential to the development of protective antisera against lethal endotoxemia.
Immunochemical Study of Hemoglobin-Free Human Erythrocyte Membranes
Authors: Howe Calderon , Lee Lucille T. 
Published: December 2022

Summary
The plasma membrane of human erythrocytes has been characterized as an antigenic entity distinct from cytoplasmic components, certain of which may be included in hemoglobin-free ghosts prepared by hypotonic lysis of erythrocytes at pH 7.4. Lyophilization and subsequent rehydration resulted in the partition of the protein in hemoglobin-free membranes between a major, insoluble fraction from which pure erythrocyte mucoid (virus receptor substance, VRS) was extractable, and a minor, soluble fraction (soluble ghost protein, SGP). The SGP fraction, free of detectable receptor activity, comprised at least four proteins, one of which cross-reacted with VRS. The latter, in quantitative precipitin, double diffusion, electrophoretic and immunoelectrophoretic analyses, behaved as a single antigen. Together with components of SGP, VRS was held responsible for the “nonspecific” agglutinins provoked in rabbits by the injection of whole erythrocytes, hemolyzates or fractions containing plasma membrane constituents. SGP components were therefore assumed to be exposed at the surface of intact erythrocytes in intimate association with mucoid which bears blood group antigens and virus receptors. The solubilization of erythrocyte membranes by means of detergents and organic solvents results in the partition of lipid, protein and polysaccharide in a manner distinctly different from that which follows lyophilization and rehydration as described in this report.
A Glycoprotein That Induces Nephrotoxic Antibody: Its Isolation and Purification from Rat Glomerular Basement Membrane
Authors: Shibata Seiichi , Miyakawa Yuzo , Naruse Takuji , Nagasawa Toshihiko , Takuma Takehide 
Published: December 2022

Summary
The water-soluble antigen that induces nephrotoxic antiserum was isolated and purified from rat glomerular basement membrane.
The highly purified antigen, Fr-αS, obtained from TR-GBM, had the character of a glycoprotein which gave a single symmetric sedimentation boundary line in the analytical ultracentrifuge (s20,w = 1.02 S).
The yield of Fr-αS was only 5.5 mg (dry weight) from 390 mg of TR-GBM, starting with 3.0 kg (wet weight) of perfused renal cortex homogenate.
Rats that received a single injection of antiserum against rat Fr-αS showed distinct clinical and histologic changes of typical proliferative glomerulonephritis, which were strikingly similar to the various stages of glomerulonephritis in man.
Use of Insoluble Antibody for Quantitative Determination of Small Amounts of Immunoglobulin
Authors: Mann Dean , Granger Harriet , Fahey John L. 
Published: December 2022

Summary
A quantitative inhibition test for individual proteins has been developed using isotopically labeled 125I protein and insoluble antibody. Antibodies, reacting specifically with individual human immunoglobulins (IgG, IgA, IgM, κ or λ), were made insoluble by coupling to bromacetyl cellulose by the technique of Robbins, Haimovich and Sela. Radioiodinated immunoglobulins were used with insoluble antibody in quantitative inhibition tests to measure the human immunoglobulins.
The test is rapid, gives reproducible results, and is more sensitive than gel diffusion precipitation assays.
Rabbit Light Chains Lacking b-Allotypic Specificities
Authors: Rejnek J. , Mage R. G. , Reisfeld R. A. 
Published: December 2022

Summary
After oxidative sulfitolysis of normal rabbit IgG, two fractions (LI and LII) of light chains were separated by gel filtration on Sephadex G 100 in acid-urea. More than half of the light chains in the LI fraction (b-n) lacked antigenic determinants associated with the b locus (b+) and shared antigenic determinants with a distinct type of light chain (b-s) previously isolated from the sera of rabbits suppressed for genetic expression of b locus allotypes. The LII fraction, representing about 80% of the total light chain population from normal b5 rabbits, was found to be largely if not entirely composed of b+ light chains. Both b-n and b-s light chains were found to be antigenically distinct from b+ light chains. This supports the hypothesis that rabbit b- light chains obtained from normal or suppressed rabbits correspond to λ type chains.
The Synthesis of Secretory IgA in the Rabbit
Authors: Lawton Alexander R. , Mage Rose G. 
Published: December 2022

Summary
Colostral IgA from rabbits heterozygous for light chain allotypic specificities controlled by the b locus has been shown by quantitative precipitin techniques to consist of molecules bearing one allelic type or the other but not both. Molecules containing both specificities were obtained by mixing b4 and b5 colostral IgA in 5 M guanidine and dialyzing away the guanidine. These observations indicate that 11 S colostral IgA is synthesized as a dimer in single cells and not derived from 7 S IgA.
Density Distribution Analysis of Cells Forming 19 S Hemolytic Antibody in the Rat
Authors: Haskill J. S. , Legge D. G. , Shortman Ken 
Published: December 2022

Summary
Hemolytic antibody-forming cells from spleen, lymph nodes, blood and thoracic duct lymph of the rat have been analyzed and in some cases purified using the technique of equilibrium density gradient centrifugation. Data on the size range distribution and kinetics of appearance have also been obtained.
The results are in accord with the pleomorphism of 19 S hemolytic antibody-forming cells established by morphologic criteria. The density distribution profiles are extremely complex and do not simply represent a continuum of components. The results provide evidence for distinct stages rather than a continuing process of development of the antibody-forming cell.
Differences in the density profiles between fixed and circulating antibody-forming cells suggest a restriction in the classes of cells that can enter the circulation.
One circulating antibody-forming component was enriched 100-fold by density separation whereas no more than two-fold enrichment was obtained with cells from spleen or the lymph nodes. The technique offers promise as an analytic approach to cell population dynamics.
Lack of Skin-Sensitizing Property of γD Myeloma Protein in Guinea Pigs
Authors: Ovary Zoltan 
Published: December 2022

Abstract
Reverse passive cutaneous anaphylaxis (RPCA) is an immediate type of reaction provoked by an initial injection of the antigen followed by injection of the antibody after a period of sensitization (1). It may be provoked in guinea pigs with antibodies of different species. It may also be provoked not only with those antibodies which can sensitize guinea pigs for PCA reactions, but also with those which cannot (1–3).
The antigen must be a γ globulin of the same class and sub-class as those antibodies which sensitize the guinea pig for PCA reactions (1, 2, 4–9). Even the Fc fragments or derivatives of the Fc fragments of these immunoglobulins obtained by coupling synthetic haptens to the Fc fragments are effective if the antibody used for challenge is against the Fc fragment or against the haptenic determinant (7, 8).
The class of γD globulins was described by Rowe and Fahey in 1965 (10).
Structural Analysis of a Slowly Sedimenting Proteolytic Fragment of Human Immunoglobulin M
Authors: Goodman Anne , Inman F. P. 
Published: December 2022

Summary
Human IgM was digested with crystalline papain in the presence of 2 × 10-3 M mercaptoethylamine for 4, 8, 12, 24 or 36 hr. A single, slowly sedimenting peak was observed in the schlieren patterns of mixtures after 8 or more hours of digestion. It was shown by immunoelectrophoresis that the protein initially constituted at least two components. One of them had some of the characteristics expected of Fabµ; the other may have been Fcµ. As the time of proteolysis increased, the latter was progressively destroyed, so that after 36 hr of digestion, only the former remained.
The identity of the papain-resistant fragment as Fabµ was based on the following observations: a) It had a sedimentation coefficient at 6 mg/ml of 3.4 S. b) Its electrophoretic migration was very slightly cathodal at pH 8.2. c) Upon gel filtration in propionic acid, the fragment was eluted in a position between that of µ chains and light chains. d) After mild reduction, the fragment dissociated into two components when gel filtered in propionic acid. One was identified as light chain and the other appeared to be a fragment of the µ chain (Fdµ).
Since Fabµ failed to dissociate in propionic acid, and was devoid of carboxymethylcysteine, the disulfide bond which joins the light chain to Fdµ remained intact during the digestive process.
Communications
Authors: Hackenthal Eberhard 
Published: December 2022

Abstract
It has been reported that sialic acid (N-acetylneuraminic acid, NANA) is an integral component of a group specific carbohydrate hapten (1) and a lipopolysaccharide (2) in Group C meningococci. Recent reports (3, 4) suggest the occurrence of sialic acid in carbohydrate antigens, presumably lipopolysaccharides (LPS), extracted from cells of serogroups A, B and C. Unpublished studies in this laboratory of LPS derived from Group B organisms have revealed that sialic acid, although present in whole cells, is not a component of their purified LPS. The positive reactions observed with hydrolysates of LPS in the thiobarbiturate (TBA) test (5) commonly used to estimate sialic acids could be attributed to the presence of keto-deoxyoctonic acid (KDO), which was identified by paper chromatography.
To clarify this situation, 19 strains of meningococci were examined as to the distribution of sialic acid and KDO in them. Each was incubated on a shaker for 18 hr in liter volumes of Mueller-Hinton broth, treated with 0.5% formaldehyde, harvested by centrifugation, washed with saline and dried with acetone.
Antibody Responses in Children and Elderly Persons Following Local or Parenteral Administration of an Inactivated Influenza Virus Vaccine, A2/Hong Kong/68 Variant
Authors: Fulk Robert V. , Fedson David S. , Huber Margret A. , Fitzpatrick James R. , Howar Bruce F. , Kasel Julius A. 
Published: December 2022

Abstract
We recently reported that the frequency and duration of serum antibody responses of elderly persons vaccinated by intranasal application of inactivated influenza virus vaccine were not significantly different from those seen following parenteral vaccination (1). The titers and duration of IgA antibody in nasal secretions were higher following nasopharyngeal vaccination than after subcutaneous immunization. The vaccine used in that study contained one type B and two type A2 components. Similar results were reported in another study with younger adults using a monovalent A2 influenza virus vaccine (2). With the introduction of a new, epidemic strain of influenza type A2 virus into an immunologically unprepared population, the responses to immunization with a vaccine containing a strain of virus representative of the type A2 variant causing outbreaks in the Far East are of special interest.
Since elderly persons experience a high mortality rate from influenza and its complications, the present study was undertaken to evaluate antibody responses following intranasal or subcutaneous administration of inactivated monovalent vaccine in this age group.
The Subunit Structure of Influenza Virus Envelope Protein
Authors: Eckert Edward A. 
Published: December 2022

Abstract
The influenza virus particle is surrounded by a lipid-protein envelope from which spike-like projections protrude. There is evidence that the major surface structural antigen is located in these projections (1). In an earlier report (2), procedures for obtaining envelope protein in a soluble form were described. Virus concentrates were extracted first with methanol-chloroform and the residue was treated with 8 m urea and 0.01 m dithiothreitol. In this solvent the envelope protein was reduced to chemical subunits, which, on removal of the dissociating reagent by dialysis, assembled into a uniform protein with a sedimentation constant of 4 S. A specific serologic relationship was demonstrated by complement fixation and blocking antigen tests between the homogeneous protein preparation and the strainspecific surface antigen of the viral envelope (2). The present report is concerned with attempts to obtain envelope protein in a more highly purified state and to determine by acrylamide gel electrophoresis the number of polypeptide components associated with the preparations.
A Comparative Antigenic Study of λE-Globulin and Myeloma-IgND
Authors: Bennich Hans , Ishizaka Kimishige , Ishizaka Teruko , Johansson S. Gunnar 
Published: December 2022

Summary
IgND, represented by a myeloma protein ND and γE-globulin, detected in and isolated from atopic patients' sera with reaginic activity, belong to the same immunoglobulin class, which is distinct from IgG, IgA, IgM and IgD.
The antigenic determinants characteristic of the fifth immunoglobulin class, which should be designated IgE, are localized in the Fc portion of the molecule.
The association of reaginic activity with IgE was confirmed by the fact that anti-γE globulin as well as an antiserum specific for the Fc portion of myeloma-IgND precipitated the reaginic factor in atopic patients' sera.
Antibodies to Herpesvirus Hominis Types 1 and 2 in the Rabbit
Authors: Nahmias André J. , Dowdle Walter R. , Kramer Joel H. , Luce Carolyn F. , Mansour S. Cleo 
Published: December 2022

Summary
The microneutralization technique and pN method of analysis were used to differentiate antibodies to Herpesvirus hominis (HVH) types 1 and 2 in the rabbit. On the basis of this and other studies, pN difference values (type 1 – type 2) higher than +0.5 were considered to represent a type 1 response, values less than +0.05 a type 2 response and values between +0.05 and +0.5 an intermediate response. In experiments in which rabbits were inoculated with one HVH type followed by injections of the other type, it appears that the intermediate response represents exposure to both HVH types.
Ocular inoculation of animals previously infected with one or the other HVH type resulted in infection of the cornea in some cases despite the presence of systemic antibodies.
Ca++-Dependent Binding of Antigen-19 S Antibody Complexes to Macrophages
Authors: Lay Waltraut H. , Nussenzweig Victor 
Published: December 2022

Summary
Mouse leukocytes have distinct membrane receptor sites for sheep red blood cells (SRBC) sensitized with either the 7 S (EA (7S)) or the 19 S (EA (19 S)) fractions of a mouse anti-SRBC antiserum. The receptors for EA (7 S) or EA (19 S) can be distinguished from each other because the binding of EA (7 S) to macrophages is inhibited by normal 7 S mouse immunoglobulins, whereas the binding of EA (19 S) is unaffected. Moreover, the binding of EA (19 S) to macrophages depends on the presence of Ca++ ions in the incubation medium while EA (7 S) adheres to leukocytes in the presence of Na3HEDTA. The receptors for EA (7 S) were found on macrophages, blood monocytes and polymorphonuclear leukocytes, while the receptors for EA (19 S) were detected only on macrophages. The receptors for both 7 S and 19 S immunoglobulins are not destroyed by trypsin treatment of the macrophages, and this property distinguishes them from the receptors for complement component(s) present on the same cells (2).
Antibody Response in Rainbow Trout (Salmo Gairdneri)
Authors: Chiller J. M. , Hodgins H. O. , Chambers V. C. , Weiser R. S. 
Published: December 2022

Summary
The rosette test was used to study the morphology of antibody-forming cells obtained from lymphoid tissue of rainbow trout after the administration of sheep erythrocytes. Phase and electron microscopy revealed that five classes of cells were capable of forming rosettes: lymphocytes, plasma cells, blast-like cells, macrophages and cells resembling eosinophils. All these types of rosette-forming cells were found in the spleen and the anterior kidney. Although a quantitative relationship between serum agglutinins and numbers of rosette-forming cells was lacking, rosettes were numerous only in lymphoid tissue of animals that demonstrated minimal hemagglutinin titers of 1:64.
Antibody Response in Rainbow Trout (Salmo Gairdneri)
Authors: Chiller J. M. , Hodgins H. O. , Weiser R. S. 
Published: December 2022

Summary
The successful application of the Jerne test to lymphoid cells from immunized rainbow trout was found to depend on the use of isologous C′ or C′ of closely related species. Of the mammalian, avian, amphibian, and fish C's tested, only sera of salmonid fish were active. Two types of plaques were seen, distinguishable by size—large plaques, 1 to 3 mm in diameter, and small plaques, 0.1 to 0.4 mm in diameter. Studies of the kinetics of plaque formation revealed that in the primary response, plaques first appeared 2 to 6 days after injection with antigen and peaked on about day 14. Plaque-forming cells were first detected in the anterior kidney.
Gel filtration of normal trout and salmon sera on Sephadex G-200 yielded a pattern with three major protein peaks; complement activity necessary for plaque formation or for tube hemolysis was limited to the second peak. The third peak contained natural hemolytic activity which was manifested after prolonged incubation with SRBC's. It was demonstrated that this natural hemolytic activity of normal serum can take place in vivo.
Studies of Immune and Normal Opsonins during Experimental Staphylococcal Infection in Rabbits
Authors: Nickerson D. Scott , Kazmierowski John A. , Dossett John H. , Williams Ralph C. , Quie Paul G. 
Published: December 2022

Summary
Antibacterial antibody response was studied in rabbits that were experimentally infected with staphylococci so as to simulate human endocarditis and osteomyelitis. Sera from rabbits inoculated intravenously twice weekly for 4 weeks contained high titers of opsonic, agglutinating, and complement-fixing antibodies. In a second group of rabbits, single intramedullary inoculations of staphylococci successfully produced osteomyelitis. These animals also developed high titers of opsonic and agglutinating antibodies. The titers of complement-fixing antibodies were generally lower in rabbits with experimental osteomyelitis than they were in animals with recurrent bacteremia. Opsonic antibodies were specifically and completely absorbed by the infecting strain of Staphylococcus aureus. No evidence was obtained for “leukophilic” γ globulin with phagocytosis-promoting activity. Sucrose gradient fractionation of immune rabbit sera indicated that the primary heat-stable opsonin was 7 S γG.