bluuebunny/crossref_metadata_2025_split huggingface dataset:
Hapten-Carrier Relationships in the Production of Rat Homocytotropic Antibodies
Authors: Strejan Gill H. , Marsh David G. 
Published: December 2022

Abstract
Various hapten-protein conjugates have been used to elicit the production of antibodies involved in immediate-type hypersensitivity reactions in immediate-type hypersensitivity reactions in guinea pigs (1, 2), mice (3), rats (4, 5) and man (6). In the guinea pig, the concentration, the relative proportions of γ1 and γ2 and the average intrinsic association constant of anti-2,4-dinitrophenyl (DNP) antibodies were shown to depend on the nature of the carrier molecule used for immunization (7). Soluble extracts derived from Ascaris suum injected in association with B. pertussis vaccine elicited high titers of homocytotropic (Hc) antibodies in the rat; compared with hemocyanin and ovalbumin, 10 times less Ascaris antigen was required to induce detectable levels of Hc antibodies (8). The present report deals with the production of rat Hc antibodies to three different dinitrophenyl-carrier conjugates. The results will show that both anti-DNP and anti-carrier antibody titers obtained in rats immunized with a DNP-Ascaris conjugate were significantly higher than those obtained against DNP-hemocyanin or against DNP-bovine gamma globulin.
Human Clr, Purification and Assay Based on Its Linking Role
Authors: de Bracco M. , Stroud R. M. 
Published: December 2022

Abstract
C1, the first component of C, has been shown to be a macromolecule composed of three subunits, C1q, C1r, and C1s. Whereas C1q and C1s have been purified and monospecific antibodies have been produced against both, the C1r preparations used in most studies were only partially purified.
We developed a method of purification and assay for C1r. The purification procedure starts with a neutral euglobulin precipitation, followed by DEAE- and CM-cellulose chromatography, and a final preparative polyacrylamide gel electrophoresis.
Rabbits injected with this preparation produce monospecific precipitating antisera, which are capable of inhibiting C1 activity of cell-bound and fluid phase C1, but do not inhibit C1q or C1s.
The electrophoretic mobility of purified C1r is that of a β globulin on disc acrylamide electrophoresis at pH 8.6; its molecular weight, as estimated by Sephadex G-200 gel filtration, is 168,000.
The hemolytic assay of C1r in purified preparations is based on its property to link C1s to C1q and thereby generate macromolecular C1.
Restriction of the Substrate Specificity of C1 Human by Heat Inactivation or Cell Binding
Authors: Kondo M. , Gigli I. , Austen K. F. 
Published: December 2022

Abstract
Fluid phase or cell-bound activated first component of human complement (C1̄) utilizes the fourth (C4) and to a lesser degree the second (C2) components, as well as N-α-acetylglycyl-l-lysine methylester (AGLMe), N-acetyl-l-arginine methylester (AAMe), p-tosyl-l-arginine methylester (TAMe) and N-acetyl-l-tyrosine methylester (ATMe). The hydrolysis of either natural or synthetic substrates is decreased when C1̄ is cell bound (EAC1̄). Inactivation of C4 and C2 by C1̄ or EAC1̄ is inhibited by TAMe and AAMe, but not ATMe. C2 destruction by C1̄ in the presence of C4 exhibits a similar inhibition profile with these esters.
Heat-inactivated C1̄ loses the ability to split C2, TAMe, or ATMe, but not C4 or AAMe. C4 destruction by heat-inactivated C1̄ is prevented by AAMe. C1̄ can be blocked by C1̄INH so as to lose its activity against C2 and TAMe, but not C4 or AAMe.
Degradation of C3b by the C3b Inactivator
Authors: Ruddy S. , Austen K. F. 
Published: December 2022

Abstract
The C3b Inactivator (C3bINA) is a normal serum β globulin which destroys the activity of cell-bound C3b in immune hemolysis, immune adherence and the enhancement of phagocytosis. C3bINA treatment of EAC14oxy23 prepared with 125I-labeled C3 releases protein-bound radioactivity into the supernatant fluid. Kinetic studies demonstrate that the rate of disappearance of the hemolytic activity of cell-bound C3b greatly exceeds the rate of release of radioactivity from the cell surface. Polyacrylamide disc electrophoresis of the products of the action of C3bINA on washed EAC1423 125I cells reveals two new radioactive bands derived from the labeled C3, in addition to traces of C3b; only traces of C3b are found in supernatants from cells incubated in buffer alone. The more prominent new band migrates anodally to C3b, in a region identical to that of C3c produced by aging radioactive C3 in whole human serum at 37°C for 48 hr; the behavior of this band on gel filtration also resembles that of C3c and this band contains the “A” antigen of C3.
C3 Consumption in Immune Reactions
Authors: Pondman K. W. , Hannema A. , Wolters G. 
Published: December 2022

Abstract
C3 consumption and site formation was studied with specific antisera against three antigenic determinants of the C3 globulin molecule, namely, [β1C] or B, the β1A and the α2D determinant.
Interaction between C3 in serum and optimal specific precipitates results in the rapid loss of the [β1C] or B determinant and concomitant appearance of C3i and free α2D in the fluid phase, the latter determinant being nearly unexposed in intact C3 globulin. Experimental data further suggest that the B determinant of the intact C3 molecule is lost by destruction or by intramolecular rearrangement in the C3 molecule after interaction with cell bound C. This is borne out by the following data. (a) Immune aggregates with bound complement are incapable of inducing anti-[β1C] antibodies in rabbits; (b) sensitized Lea-positive red cells with bound complement agglutinate with monospecific anti-α2D and anti-β1A, but fail to agglutinate with anti-[β1C]; (c) EAC1̄, cells prepared with limited C3 fail to agglutinate with anti-[β1C] but agglutinate strongly with anti-β1A and anti-α2D.
Additional Studies on the Fractionation of Human C5: Identification, Possible Method of Removal and Significance of a Plasminogen/Plasmin Contaminant
Authors: Nilsson U. R. , Tomar R. H. , Taylor F. B. 
Published: December 2022

Abstract
Preparations of C5 purified according to a previously described preparation procedure (Nilsson and Müller-Eberhard, 1965) demonstrated fibrinolytic activity when reacted with streptokinase in a bovine clot lysis assay. Fibrinolytic activity was readily demonstrable although quantitative analysis revealed that the degree of contamination would correspond to only 0.01% to 0.05% plasminogen/plasmin (Plg/Pln). Presence of a potentially active proteolytic enzyme in the C5 fractions may cause uncontrolled modification of the C5 protein. Loss of C5 hemolytic activity upon treatment with relatively large doses of Pln supports this possibility. Attempts have been made to accomplish a complete separation of C5 from Plg/Pln, as well as to prevent possible proteolytic action by Pln during the purification procedure.
A Blood Coagulation Abnormality in C6 Deficient Rabbits and Its Correction by Purified C6
Authors: Zimmerman T. S. , Arroyave C. M. , Müller-Eberhard H. J. 
Published: December 2022

Abstract
In this communication we report a coagulation abnormality in rabbits genetically deficient in the sixth component of complement which is characterized by prolonged whole blood clotting time and deficient prothrombin consumption. The mean glass clotting time in five C6 deficient rabbits was 38 min (range: 34 to 41 min) as opposed to a mean of 24 min (range: 20 to 31 min) in five normal rabbits. Clotting times in plastic tubes varied from 140 to over 400 min in C6 deficient animals, whereas the range for the normal rabbits was 70 to 90 min. Prothrombin consumption measured in plastic tubes for 1 hr at 37°C varied from 0% to 10% in six deficient rabbits, whereas the mean for six normal rabbits was 72.5% with a range of 62% to 79%. Prothrombin and partial thromboplastin times were normal in the deficient animals as were activities of the classical clotting factors II, V, VII, VIII, IX, X, XI and XII.
Arrangement of Macromolecular Components in Erythrocyte Membranes and Their Relation to Bound C3 and C4
Authors: Dalmasso A. P. , Diaz A. , de Bracco M. M. E. 
Published: December 2022

Abstract
The purpose of this study was to examine the distribution of a ntigenic components in the intact erythrocyte (E) membrane (M) and their relation to bound C3 and C4. Rabbit antisera were prepared by immunization with whole sheep EM. Immunoelectrophoresis (IEP) of M solubilized with 2.5% Triton X-100 (T) revealed one β2 line and two to four α-β1 lines. M solubilized by sonication in 10% n-butanol and fractionated by ultracentrifugation in 24% sucrose (Morgan, T. H. and Hanahan, D. J., Biochemistry, 5: 1050, 1966) yielded a light fraction rich in carbohydrates and lipids, having high affinity for T and β2 position on IEP after treatment with T, and a heavy fraction rich in protein, migrating in the α-β1 IEP area. Absorption of anti-EM with intact E removed its hemagglutinating activity and its capacity to react with the β2 component without altering its anti α-β1 activity.
Complement-Mediated Lysis of Nucleated Cells
Authors: Shipley U. W. , Baker A. R. , Colten H. R. 
Published: December 2022

Abstract
The availability of a rapidly growing cell line in tissue culture (Chinese hamster lung, CHL) with high plating efficiency and the ability to form discrete colonies has made it possible to adapt the colony inhibition technique to quantitative studies of complement-mediated lysis of nucleated cells and, in particular, to study the effect of the cell growth cycle on the susceptibility of target cells to immune lysis. During complement-mediated lysis, the cells were examined by phase contrast microscopy, the molecular weight of target cell DNA was estimated by ultracentrifugation in alkaline sucrose gradients and the extent of lysis was determined by a loss of colony-forming ability.
Within 8 min after the addition of complement to sensitized CHL cells, morphologic changes in the target cells were noted. Following these changes, an enzymatic degradation of target cell DNA occurred, resulting in a 10-fold reduction in molecular weight of the single-stranded DNA fragments.
The Immune Response in the Hamster
Authors: Coe J. , Peel L. , Smith R. F. 
Published: December 2022

Abstract
Hamster 7Sγ1 and 7Sγ2 antibodies to hen-egg albumin (HEA) were tested for their ability to fix complement and mediate passive cutaneous anaphylaxis (PCA). Only 7Sγ2 anti-HEA bound complement in the micro-complement-fixation test and hemolysed HEA-sensitized sheep red blood cells. In addition, only 7Sγ2 anti-HEA mediated the PCA reaction in guinea pigs, which could be blocked with 7Sγ2 globulin from normal hamster sera. Hamster antibody did not produce detectable PCA reactions in hamsters, and hamsters with circulating 7Sγ1 anti-HEA did not show signs of active anaphylaxis after intravenous challenge with the antigen.
Genetic Polymorphism in Rhesus C3 and Ge Globulin
Authors: Alper Chester A. , Robin Noel I. , Refetoff Samuel 
Published: December 2022

Abstract
Extensive genetic polymorphism of C3 was found in 81 sera from rhesus monkeys. Evidence was obtained for three alleles, rhesus C3S, C3F and C3F1, with gene frequencies of 0.66, 0.33 and 0.01. The variants were inherited as autosomal codominant traits. Polymorphism of Gc globulin was also found. Although most sera contained Gc globulin that formed a single band on electrophoresis, in a few sera this protein consisted of two bands, one of which was slower than the usual. These observations suggested that Gc globulin was controlled by two codominant alleles, rhesus Gc1 and Gc2, with frequencies of 0.975 and 0.025, respectively.
Antibody Formation Against Salmonella Flagella by an Immune Ribonucleic Acid Fraction
Authors: Yamaguchi Nobuo , Kurashige Satonori , Mitsuhashi Susumu 
Published: December 2022

Abstract
An immune ribonucleic acid (RNA) preparation was extracted with phenol from the spleens of mice immunized with Salmonella flagella. A high titer of serum antibody was produced after injection of only a small amount of Salmonella flagella into mice that had previously been injected with immune RNA. This reaction was found to be immunologically specific and indicated a secondary antibody response. In contrast, secondary responses were not induced by injection of an immune RNA preparation into mice primed with either an immune RNA preparation or Salmonella flagella. These results suggest that immune RNA preparations did not contain antigens or fragments thereof, or at least the antigens that are needed to stimulate a secondary response. They indicated, moreover, that the immune RNA preparation can induce memory cells capable of responding to a secondary antigenic stimulus. The required interval between first and second antigenic stimulation and the necessary amounts of immune RNA or flagella antigen were investigated.
Effect of Cold Exposure on the Immunologic Response of Rabbits to Human Serum Albumin
Authors: St. Rose J. E. M. , Sabiston B. H. 
Published: December 2022

Abstract
The effect of low environmental temperature on the response of rabbits to a single injection of human albumin was examined. Animals exposed to cold (4°C ± 2°C) had faster catabolism of antigen and earlier appearance and higher levels of circulating antibody. Mercaptoethanol-resistant antibody was produced early (12 days) in coldexposed animals and late (26 days) in non-exposed animals. The effects of cold exposure on the immune response were as apparent after acute exposure (1 to 2 days) as after chronic exposure (3 to 8 wk).
Inability of the NZB/NZW F1 Thymus to Transfer Cyclophos-Phamide-Induced Tolerance to Sheep Erythrocytes
Authors: Jacobs Michael E. , Gordon Joyce Kay , Talal Norman 
Published: December 2022

Abstract
NZB/NZW (B/W) and C57BL/6 mice were made tolerant to sheep erythrocytes with cyclophosphamide. Thymus or bone marrow cells from tolerant or untreated donors were injected in various combinations into syngeneic irradiated recipients and assayed for plaque-forming cells. In C57BL/6 mice both marrow and thymus transfer tolerance; however, in B/W mice only the bone marrow did so. Unexpectedly, the B/W thymus from tolerant donors cooperated fully with B/W marrow cells from untreated donors. Thus the B/W thymus did not express the donor animal's tolerance status.
Immunochemical Studies on Bovine Carboxypeptidases a
Authors: Amiraian Kenneth , Plummer Thomas H. 
Published: December 2022

Abstract
Rabbit antisera to bovine carboxypeptidase Aγ were prepared by intravenous injection of a crystalline suspension of the enzyme. Quantitative immunoprecipitation tests with these antisera and carboxypeptidases Aγ and Aα and procarboxypeptidase A show that carboxypeptidase Aα, which possesses seven additional amino acids in the amino terminal position compared with carboxypeptidase Aγ, precipitates 10% less antibody N than does the homologous antigen. Procarboxypeptidase A precipitates only 8% to 15% of the antibody N as carboxypeptidase Aγ, and the proenzyme is maximally precipitated at the same weight of N rather than at the same molar concentration as the enzyme. Immune precipitates formed with carboxypeptidase Aγ and rabbit anticarboxypeptidase Aγ sera, at equivalence, are almost as active as the free enzyme in hydrolyzing carbobenzoxyglycyl-L-phenylalanine. These precipitates are capable, to a lesser degree, of hydrolyzing the carboxy terminal amino acids of human and bovine serum albumins. Immune precipitates formed with bovine carboxypeptidase B and its rabbit antisera, at equivalence, are as active as the free enzyme toward the substrate hippuryl-L-arginine.
Immunochemistry of the Cell-Wall Carbohydrate of Group L Hemolytic Streptococci
Authors: Karakawa W. W. , Wagner J. E. , Pazur J. H. 
Published: December 2022

Abstract
A cell-wall carbohydrate consisting of N-acetylglucosamine, N-acetylgalactosamine, galactose and rhamnose was isolated from group L hemolytic streptococci. The antigenic determinant of this carbohydrate consisted of terminal β-N-acetylglucosamine residues attached to rhamnose side chains of the polymer. Group L carbohydrate treated with an induced enzyme preparation from a soil bacterium no longer gave a precipitin reaction with its homologous antiserum but did so strongly with antigroup G streptococcal serum. The native carbohydrate also gave a precipitin reaction with antisera from rabbits immunized with group A streptococci. The antigenic cross-reactivity between group A and group L carbohydrates was due to the fact that the antigenic determinants of both carbohydrates were terminal β-N-acetylglucosamine residues. The N-acetylglucosamine residues of group L carbohydrate were extremely acid labile, whereas those of the group A carbohydrate were considerably more stable. This difference indicated some subtle structure differences between group A and group L antigens.
Distribution of H-2 Alloantigenic Specificities on Radiolabeled Papain-Solubilized Antigen Fragments
Authors: Cullen Susan E. , Nathenson Stanley G. 
Published: December 2022

Abstract
A method for determining the distribution of H-2 alloantigenic specificities on papain-solubilized fragments has been developed. Partially purified, radiolabeled antigen was reacted with monospecific alloantiserum and the antigen-antibody complex was removed by gel filtration or disc gel electrophoresis. Several specificities were shown to reside on the same fragment because monospecific sera removed specificities in addition to the one against which each serum was directed.
In Vitro Studies of the Human Response to Organ Allografts: Appearance and Detection of Circulating Activation Lymphocytes
Authors: Hersh Evan M. , Butler William T. , Rossen Roger D. , Morgan Robert O. , Suki Wadi 
Published: December 2022

Abstract
The rate of 3H-thymidine incorporation into circulating peripheral blood lymphocytes was measured immediately after isolation from the blood of 24 organ allograft recipients followed serially, and 42 normal control subjects. The isotope incorporation by 106 cells incubated for 2 hr with 2 µCi of 3H-thymidine was referred to as the activated lymphocyte level. It was 319 ± 295 (mean ± standard deviation) counts per minute (cpm) in the normal controls, 535 ± 377 cpm in the patients prior to grafting, 644 ± 629 cpm after grafting but when the patients had adequate nonfluctuating graft function, and 6744 ± 3798 cpm during active rejection characterized by progressively decreasing graft function. Levels rose an average of 5.4 days prior to clinical signs of rejection and tended to remain high for an average of 10.9 days after rejection was controlled, as characterized by stabilization or improvement in graft function. This outpouring of dividing lymphoblasts was interpreted as the production of effector cells in response to the antigenic stimulus of the graft. Its identification may be useful to predict impending rejection.
Regulation of Homocytotropic Antibody Formation in the Rat
Authors: Taniguchi Masaru , Tada Tomio 
Published: December 2022

Abstract
The effects of four representative immunosuppressants, i.e., 5-bromouridine deoxyriboside (BUDR), actinomycin D, cyclophosphamide and cortisone, on the formation of homocytotropic antibody (HTA) were observed in rats immunized with dinitrophenylated ascaris extracts (DNP-As) and killed Bordetella pertussis, with the following results. 1) A single injection of 35 mg/kg of BUDR given simultaneously with or shortly after the start of immunization caused enhancement and prolongation, after some delay, of HTA formation, as measured by the mean of reciprocal PCA titers. 2) Pretreatment with 0.3 mg/kg of actinomycin D caused a delayed response of HTA, but the subsequent mean peak titer was about the same as that of the control untreated rats. Such treatment after immunization was started caused an absolute stimulation of HTA, as judged by high peak titers and prolonged production of the antibody. 3) Pretreatment with a single injection of 150 mg/kg of cyclophosphamide caused delayed but enhanced formation of HTA which lastedo lnger than the normal period of time, whereas the same treatment started 2 days after the antigen was given caused suppression. 4) Pretreatment with 200 mg/kg of cortisone caused temporary enhancement, whereas treatment during immunization was moderately suppressive. The enhancement or suppression of HTA formation did not correlate with γM and γG antibodies in the serum, as measured by passive hemagglutination titers before and after 2-mercaptoethanol treatment.
Long-Term Reconstitution of Bursectomized Chickens
Authors: Cain W. A. , David L. A. 
Published: December 2022

Abstract
Since the discovery of the immunologic role of the avian bursa of Fabricius (1), several investigations (2–4) have succeeded in defining functions of this organ. Bursectomy before hatching (5, 6), treatment of embryos or young chicks with testosterone (7) or cyclophosphamide (8), and bursectomy on the day of hatching coupled with whole body x-irradiation (9) block development of bursa-dependent components of peripheral lymphoid tissues.
In later life, chickens bursectomized by one of these methods are deficient in immunoglobulins, lymphoid germinal centers, plasma cells and the ability to make antibodies. It can be concluded that the bursa of Fabricius is the central lymphoid organ in chickens, which performs crucial steps in the development of humoral immunologic competence.
Less progress has been realized in attempts to define mechanisms of bursal action.
A Simplified Method for Measuring Human IgE
Authors: Centifanto Ysolina M. , Kaufman Herbert E. 
Published: December 2022

Abstract
The radioactive single radial diffusion test described by Rowe (1) is commonly used for determining human IgE in secretions. Although this test is sensitive and allows the measurement of IgE at amounts as low as 40 ng/ml, it has definite drawbacks. First, extensive washing is necessary to remove both unreacted sheep antihuman IgE and 131I-labeled rabbit antisheep globulin serum. Second, the short half-life of the radioactive label makes this test impractical for routine diagnostic measurements of IgE in secretions or sera.
Another test described by Arbesman and Ito (2) uses a one-step reaction with 125I-labeled antihuman IgE serum, thus eliminating the need to use antibodies to anti-IgE.
Although both tests are sensitive and very suitable for research projects, a simplified procedure that does not require radioactive labeling seemed desirable. For this purpose, we developed a new method to detect IgE in human tears, which employs a fluorescein-labeled rabbit antisheep globulin reagent.
Characterization of Immunoglobulin G Anti-Glomerular Basement Membrane Antibodies Eluted from Kidneys of Patients with Glomerulonephritis
Authors: McPhaul John J. , Dixon Frank J. 
Published: December 2022

Abstract
Direct immunofluorescence microscopy was performed on sections of kidney from 22 patients with anti-glomerular basement membrane (anti-GBM) antibody-mediated nephritis proved by in vitro elution techniques. Although immunoglobulin G (IgG) was fixed to glomeruli of all native or transplanted kidneys, the third component of complement (C3) was bound at the site of IgG fixation in slightly more than half (10 of 17). Immunoglobulin subtyping of eluted IgG anti-GBM antibodies, performed by an indirect immunofluorescence technique, indicated the presence of IgG subtypes 1, 2 and 3 in the eluates. Although eluted IgG anti-GBM antibodies failed to fix human C3 on normal homologous kidney sections, IgG anti-GBM antibodies isolated from serum of nephritic patients did so. Failure to visualize C3 by immuno-fluorescence examination of nephritic human kidneys was usually not due to an anomaly of IgG subtype participation or to lack of intrinsic ability of IgG anti-GBM antibodies to bind C3 in vitro.