bluuebunny/crossref_metadata_2025_split huggingface dataset:
Comparative Study of Antibodies to Native and Denatured DNA
Authors: Tan E. M. , Natali P. G. 
Published: December 2022

Abstract
Serum from a patient with systemic lupus erythematosus (SLE) containing antibodies to native DNA was compared with antiserum from a rabbit immunized with heat-denatured DNA. DNA was fractionated on methylated albumin kieselguhr into native and denatured forms, which were used as antigens in immunologic tests. By immunodiffusion, complement fixation and immunofluorescence, rabbit antiserum reacted only with denatured DNA and was completely unreactive with native DNA. SLE serum reacted strongly with native DNA in all tests and weakly with denatured DNA in complement-fixation and immunofluorescence tests. These studies demonstrated the importance of employing purified preparations of native or denatured DNA to differentiate between DNA antibodies of different specificities. They also showed that DNA antibodies experimentally induced by immunization with heat-denatured DNA did not cross-react with purified native DNA. An immunofluorescence test was described which showed that antibodies to native DNA stained DNA in the form of strands, and antibodies to denatured DNA stained DNA in the form of aggregated granules.
Intracellular Distribution of Immunoglobulin Heavy and Light Chains Within Tissue Cultured Cells of Human Lymphoid Origin Detected by Electron Microscopy
Authors: Suzuki Ikuo , Takahashi Morinobu , Kamei Hideo , Yamamoto Tadashi 
Published: December 2022

Abstract
The ultrastructural localization of α heavy and κ light chains of immunoglobulin within lymphoblastoid cells of a human long term culture line, RPMI 4666, was studied by a combination of electron microscopy and immunocytochemistry. When cells were treated with peroxidase-conjugated antibodies that were monospecific for α chain or κ chain, and they were revealed cytochemically, the ultrastructural site of immunoglobulin accumulation was demonstrated as conspicuous electrondense precipitates within the cytoplasm of about 30% of the total cells.
In positive cells the κ chain was localized to the ergastoplasm, its membrane, the external layer of the nuclear membrane, and above all to ribosomes lining the ergastoplasmic membrane and the vicinity of the nuclear envelope.
On the other hand, the dominant site of α chain accumulation was in clusters of cytoplasmic polysomes, although α chain was also detected on the external layer of the nuclear envelope and on ribosomes associated with the ergastoplasmic membrane and nuclear envelope. Generalized staining of the cytoplasm suggesting diffusion of synthesized immunoglobulin to the cell surface, as reported with antibody-forming lymphoblasts in hyperimmunized animals, was never demonstrated in the present system.
The differential distribution of heavy and light chains suggests that they are formed separately at different sites and subsequently combined to each complementary chain prior to secretion even in lymphoblastoid cells.
Reaginic Activity Associated with Immunoglobulins Other than IgE
Authors: Reid Robert T. 
Published: December 2022

Abstract
Absorption studies using antisera to the Fc portion of the IgG molecule isolated from cord sera demonstrated that human reaginic activity belongs to more than one class of immunoglobulin. The data indicated that at least two types of protein carried reaginic activity, one of which was not an IgE immunoglobulin and probably was IgG. The non-IgE type had an intradermal half-life and latency period similar to that of IgE, and was destroyed by heating to 56°C for 4 hr.
The Antigenic Properties of Extracts of Horse Dander
Authors: O'Brien D. P. 
Published: December 2022

Abstract
It has been shown in previous papers by Longcope, O'Brien and Perlzweig (1) (5) that two proteins, precipitating out of colloidal solutions at different iso-electric points, can be isolated from crude extracts of horse dander; and that these proteins act as antigens in guinea-pigs and can be sharply differentiated biologically by anaphylactic reactions.
The following observations deal with skin reactions obtained with these various proteins of horse dander in patients allergic to horse emanations.
Two methods have been employed in the study of these extracts: first, direct tests have been made on the skin of patients who are subject to horse asthma; and, secondly, tests have been done to determine whether these extracts will call forth reactions in an area of skin of a normal individual which has been passively sensitized, according to the method of Prausnitz and Küstner (2), by the injection of serum from a patient allergic to horse dander.
Intestinal Uptake of Macromolecules
Authors: Walker W. A. , Isselbacher K. J. , Bloch K. J. 
Published: December 2022

Abstract
Rats were parenterally immunized with bovine serum albumin (BSA) and horseradish peroxidase (HRP) emulsified in complete Freund's adjuvant; absorption of these antigens was tested in vitro by means of the everted gut sac technique. A significant and specific decrease in uptake of BSA was noted in rats injected five times with BSA, but not in rats injected only twice. Absorption of 125I-HRP and HRP, measured enzymatically, was also significantly inhibited in rats immunized five times with HRP. The binding of 125I-BSA to intestinal secretions, mucosal extracts and serum from rats showing interference with BSA absorption (multiple injections) was 2- to 10-fold greater than that of comparable preparations from rats which did not show interference (injected twice). Antigen-binding to IgGa, IgG1, and IgM antibodies was demonstrated by radioimmunoelectrophoresis in the serum of rats with multiple injections of BSA; in addition, binding to IgGa and IgG1 antibodies was demonstrated with mucosal extracts. Although antigen uptake was inhibited in rats immunized parenterally with BSA and HRP, the number of gut sacs showing an inhibited response and the extent of the response were less than that previously observed with gut sacs obtained from rats immunized orally with the same antigens. Binding activity of 125I-BSA in mucosal extracts from this latter group of rats was the same as in rats parenterally immunized but only IgG1 antibodies were noted in mucosal extracts. It was suggested that the more consistent inhibition of antigen uptake in orally immunized vs parenterally immunized rats may be related to the type or pattern of local antibody distribution.
Cross-Reactions Among Group A Streptococci
Authors: Myoda T. Timothy , Wiley Grove G. , Bruno Pauline N. 
Published: December 2022

Abstract
The strain-specific (Sp-M) and the cross-protective (X-M) antigens of type G1 cocci were isolated from RNase-treated cell walls and purified by ammonium sulfate fractionation, carboxymethylcellulose and Sephadex G-200 column chromatography and polyacrylamide gel electrophoresis. Acid hydrolysis resulted in fragmentation of the antigen molecules, but precipitin and bactericidal tests established that the major serologic activity characteristic of the native antigens, with minor exceptions, remained intact. The purified antigens absorbed their corresponding antibodies to yield specific antisera whose bactericidal activity correlated with bands of precipitate in agar gel diffusion tests. It was established that the X-M antigen has specific as well as cross-reactive activity, a determination which it was impossible to make before the purified material became available.
The purified antigens with which antisera were absorbed had a ratio of O.D. 280 nm to O.D. 260 mn of 0.79 for the Sp-M and 1.00 for the X-M. The molecular size of the Sp-M was greater and the charge smaller than those of the X-M. Also, it contained twice as much glycine and half as much aspartic acid. The average ratio of lysine and arginine for the Sp-M and X-M was 2.3 and 1.5, respectively. The observation is of interest because it has been established in other work that the Sp-M requires a free ε-NH2 group of lysine and a free guanidino group of arginine for its serologic activity. The X-M antigen does not.
The antigens were extractable as separate entities at pH values from 2 to 10 and at temperatures of 37°C and 100°C, thus demonstrating that they do not arise only by acid hydrolysis of a larger molecule with Sp-M and X-M serologic activity and may indeed exist as separate antigens on the cell wall. The molecules in alkaline extracts were larger than those in acid extracts. Acid hydrolysis of the alkaline preparation yielded products whose gel electrophoretic pattern was similar to that of the acid-extracted material. Therefore, it was possible to conclude that the smaller molecules of the latter were the result of acid hydrolysis and not the other procedures employed.
T Cells Can Bind Antigen via Cytophilic IgM Antibody Made by B Cells
Authors: Webb Susan R. , Cooper Max D. 
Published: December 2022

Abstract
The specificity of cell-mediated immune responses presupposes the existence of an antigen recognition unit associated with those cells responsible for this type of immunity. Evidence is accumulating which indicates the presence of immunoglobulins on thymus-dependent lymphocytes (T cells)2 and suggests that these may represent the recognition units (1–10). Much of the supporting evidence was obtained from studies in which anti-immunoglobulin reagents inhibited antigen binding by T cells as detected by direct (autoradiography and erythrocyte rosette formation) and indirect (e.g., highly radioactive antigen-induced “suicide”) techniques. Most of these studies were done in mice; in all instances the T cells studied had been associated in vivo with bone marrow dependent (B) cells and their immunoglobulin products.
Agammaglobulinemic (Aγ) chickens represent an animal model particularly well suited to studies involving T lymphocytes since they completely lack B cells and circulating immunoglobulins but have normal T cell development and cell mediated immunity.
Serologic Assay of HL-A Antigens in the Presence of Detergents
Authors: Dawson Jeffrey R. , Shasby Sandra S. , Amos D. Bernard 
Published: December 2022

Abstract
Although several investigators have suggested that detergent extraction of the membrane bound HL-A transplantation antigens would be a useful preparative method (1–4), technical problems involved in the use of detergents have somewhat limited their use. Since these antigens are usually insoluble in the absence of detergent (2, 3), the serologic activity of the detergent-solubilized antigens must be assayed in the presence of the detergent. Therefore, if the biologic activities thought to be associated with the serologically-defined antigens are to be tested by in vitro methods, the detergent concentration must be reduced below cytolytic doses. This report demonstrates that the serologic activity of solubilized membrane antigens can be quantitated in the presence of detergents with a modified 51Cr release cytotoxicity method (5).
Methods and Materials. A stable tissue culture cell (IM1, Dr. D. L. Mann, National Institutes of Health, Bethesda, Md.) which has a phenotype of HL-A 3, 12, W27 was utilized (5).
Genetic Defects Affecting C3 Associated with Increased Susceptibility to Infections
Authors: Alper Chester A. , Rosen Fred S. 
Published: December 2022

Abstract
Since C3 occupies a crucial position in the C and properdin systems, it is understandable that defects affecting this protein produce decreased resistance to infection. We have studied three patients: 1) a 15-year-old female with homozygous deficiency of C3 whose serum C3 concentration was 1/1000th or less than normal, 2) a 27-year-old male with type I essential hypercatabolism of C3 who is homozygous for deficiency of C3 inactivator (KAF) resulting in activation of GBGase, consumption of properdin factor B, and secondary deficiencies of C3 and CVF-binding protein, and 3) a 35-year-old female with type II essential hypercatabolism of C3 who has a circulating enzyme, C3ase, that is not , not a known component of the properdin pathway, nor a known coagulation factor. The activity of C3ase is enhanced by a protein of normal serum, C3ase cofactor.
All three patients have defective serum Cmediated functions.
C Activation in Skin Disease
Authors: Provost T. T. , Tomasi T. B. 
Published: December 2022

Abstract
Monospecific antisera to human properdin, C3 proactivator (C3PA), C1q, C4, C3, C5, IgA, IgM, IgG, and IgE were employed in immunofluorescent studies of various skin diseases.
Immunofluorescent studies of skin biopsies of 25 patients with systemic lupus erythematosus (SLE) demonstrated the deposition of immunoglobulins and C components in “normal” skin biopsy specimens of 20 of these patients. Five of these patients had deposition of properdin, C1q, C4, C3, and C5, as well as various immunoglobulins, and three also had C3PA deposition along the basement membrane (BM).
Ten of 10 patients with bullous pemphigoid demonstrated C1q, C4, C3, C5, C3PA, properdin and IgG deposition along the BM.
Six patients with dermatitis herpetiformis had IgA granular deposition in the dermal papilla beneath the BM. Three of these patients also showed C3PA deposition and one patient's biopsy had positive properdin staining. Three patients with active disease were found to have C3 deposition in the absence of C1q or C4.
Participation of C in an Experimental Model of Intravascular Coagulation
Authors: Dalmasso Agustin P. , Lee Ming , Giraudo Luis A. , Swaim William R. 
Published: December 2022

Abstract
The role of C in the production of intravascular coagulation was investigated by infusing brain thromboplastin (Tpl) into normal and C-deficient (def) rabbits and mice. Measurements were made of clotting and fibrinolysis factors. In normal rabbits, Tpl infusion reduced the peripheral blood platelets to 61% of preinfusion levels. In contrast, platelets were 20% above preinfusion values in C6-def rabbits. C6-def rabbits reconstituted with purified rabbit or human C6 had a thrombocytopenic response similar to, or even greater than, that of normal rabbits. After administration of Tpl into mice, platelets were reduced to 40% of preinfusion values in B10.D2-new line (normocomplementemic) but only to 78% in B10.D2-old line (C5 def). Administration of purified human C5 to C5-def mice restored the Tpl-induced thrombocytopenia to a degree identical with that of normals. The thrombocytopenic response to C5-def mice could be enhanced to approach that of normals by infusing concentrated mouse Tpl.
Coagulation Related Deficiencies of Early Components of C (C1, C4, C2) in Human Serum
Authors: Glovsky M. M. , Alenty A. 
Published: December 2022

Abstract
During the past 2 years we have studied the serum of a 48-year-old asymptomatic barber (R. G.) who has 0 CH50 hemolytic C activity. Hemolytic assays of the individual serum components C1–C9 reveal 1 to 5% C1, C4, and C2 and normal activity of C3, C5, C6, C7, C8, and C9. C1 esterase inhibitor titers are only partially reduced and C3 PA protein is normal. Qualitative immunoelectrophoresis analysis of serum C1q, and Ouchterlony determinations of C1r and C1s appear normal as well. When R. G. plasma, with 10 units/ml heparin, EDTA, or citrate as anticoagulants, is used C activity is spared. CH50 hemolytic activity is 60% of normal and C4, C2 are only partially reduced. C1 hemolytic activity in plasma is &lt;1%. Since plasma rendered a protective effect on C4, C2, we wondered whether an abnormality in the coagulation sequence could account for this observation.
Mechanisms of Increased Susceptibility to C Lysis of Abnormal Human Red Blood Cells
Authors: Rosse W. F. , Adams J. P. , Logue G. L. 
Published: December 2022

Abstract
The cells of patients with paroxysmal nocturnal hemoglobinuria (PNH) and hereditary erythroblastic multinuclearity with positive acidified serum test (HEMPAS) are abnormally susceptible to lysis by C and cold-reactive antibodies, but for different reasons. For PNH cells, the fixation of antibody, C1 and C4 is the same as for normal cells. However, the amount of C3 fixed/C4 is increased 3- to 7-fold. The amount of C3 fixed for a given degree of lysis is about one-third that of normal cells. In a less sensitive variant of PNH cells, the amount of C3 fixed/C4 was about the same as for the markedly abnormal cells, but the amount of C3 fixed for a given amount of lysis was the same as for normal cells. Normal cells treated with sulfhydryl-reactive agents resembled PNH cells in these reactions.
HEMPAS cells fix 2 to 3 times as much of some, but not other, examples of anti-I. The amount of C1 fixed/Ab is normal.
Biologically Active C5 Production by C5 Deficient Mice After Cytogenetic Manipulation
Authors: Synderman Ralph , Levy Nelson 
Published: December 2022

Abstract
B10.D2/Sn “old” mice are genetically devoid of C5 and have an increased susceptibility to infection as well as an abnormal acute inflammatory response. B10.D2/Sn “new” mice have normal C function. Our studies showed that normal splenic macrophages produced C5 in vitro while normal murine kidney, brain, liver cells, lymphocytes and fibroblasts did not. We previously restored in vivo hemolytic C activity to C5 deficient (“old”) mice by intravenous (i.v.) administration of hybrid cells formed from “old” spleen cells and either C5 normal (“new”) kidney cells or nucleated chick erythrocytes (Levy and Latta, Nature, New Biol., 229: 51, 1971). In the present study we demonstrate the restoration of biologically active C5, MuB1 antigenicity (determined by R. Lieberman) and suggest genetic mechanisms involved in murine C5 deficiency. Cell hybridization was accomplished with inactivated Sendai virus.
Properties of Radiolabeled Rabbit C1q
Authors: Volanakis John E. , Stroud Robert M. 
Published: December 2022

Abstract
Rabbit C1q was purified from fresh serum through two successive euglobulin precipitation steps in low ionic strength EDTA buffers. The purified protein showed one band on acrylamide electrophoresis and had a specific hemolytic activity of 2 ng N/SFU (site-forming units). Functional integrity was also tested by agglutination of tanned red cells coated with aggregated γ-globulin. Inhibition of this agglutination reaction was observed with γ-globulin, DNA and endotoxin. Labeling with 125I was performed with chloramine-T in a 1:50 ratio followed by filtration on Sephadex G-25 to remove unreacted 125I and chloramine-T. The labeled protein (C1q*) had a specific radioactivity of 21.7 µCi/µg N, as determined by RID (radioimmunoassay). About 89% of the radioactivity was protein bound as determined by precipitation in 10% TCA. The labeled material retained only 20% of its original hemolytic activity. Incubation of C1q* with EA 1 × 109/ml in EDTA buffer, RSC 0.07 resulted in minimal binding of the label to the cells, while 25% binding was observed in the presence of 10-3 M Ca++.
Abnormal Levels of the Chemotactic Factor Inactivator in Human Sera
Authors: Ward P. A. 
Published: December 2022

Abstract
As shown previously, normal human serum contains a chemotactic factor inactivator (CF-I) which irreversibly inhibits chemotactic activity associated with C-derived (C3 and C5 fragments, C) and C independent (bacterial) chemotactic factors. Sera from patients with Hodgkin's disease or Bruton-type agammaglobulinemia have elevated levels of CF-I. When these sera are activated with zymosan, significantly less chemotactic activity is generated when compared with similarly treated normal human serum. For reasons that are not clear, Hodgkin's sera are lacking in CF-I activity for the C3 chemotactic fragment. A contrasting situation is found in sera from patients with deficiency of α1 anti-trypsin; their sera also lack CF-I activity. Correspondingly, zymosan activation of these sera results in significantly greater generation of chemotactic activity. The deficiency of CF-I in these sera is not due to a blocking factor, as demonstrated by retention of CF-I activity that has been added to these sera.
Secondary Structural Properties of Anaphylatoxin Preparations and Chemotactic Activity for Neutrophils
Authors: Wissler Josef H. , Stecher Vera J. , Sorkin Ernst 
Published: December 2022

Abstract
Classical anaphylatoxin (CAT), often demonstrated to be a split product (C5a) of C5, acts as catalytic component of the binary leukotactic serum peptide system (ACL-system) with cocytotaxin (CCT) as regulatory component (1). Both peptides, obtained in the crystalline state, do not attract significantly neutrophils (N). CAT displays chemotactic activity for N only when CCT is present. Investigations on the mechanism of chemotactic action of the ACL-system have evaluated that CCT acts within the ACL-system as Bronsted or Lewis acid inducing a reversible secondary structural transition in the CAT molecule (2). In view of the acidic function of CCT, we studied the secondary structural transitions (denaturation) of CAT by treatment and storage at low pH-values established by non-protein Bronsted acids, e.g., CH3COOH.
The chemotactically inactive CAT is rendered chemotactically active for N, with or without CCT, under the following conditions: storage in 0.02 N CH3COOH (-20°C), treatment at +20°C by solution in 0.5 N or 50% (v/v) CH3COOH.
Antigen-Induced Proliferation of Guinea Pig Lymphocytes in Vitro: Obligatory Role of Macrophages in the Recognition of Antigen by Immune T-Lymphocytes
Authors: Waldron James A. , Horn Robert G. , Rosenthal Alan S. 
Published: December 2022

Abstract
Highly purified lymphocytes were obtained from the lymph nodes of CFA-immune guinea pigs. Cultures of these lymphocytes did not exhibit proliferative responses upon stimulation with purified protein derivative (PPD), although they were quite responsive to stimulation with phytohemagglutinin. Addition of macrophages to these cultures resulted in marked enhancement of the PPD-induced lymphoproliferative response, but did not affect lymphocyte responsiveness to phytohemagglutinin. The ability of the purified immune lymphocytes to interact directly with soluble PPD was examined by incubating the cells for 1 hr at 37°C with various concentrations of PPD. The lymphocytes were then washed to remove unbound antigen and placed in culture. Addition of macrophages to cultures of antigen-pulsed lymphocytes did not result in the significant DNA synthesis, suggesting that the specifically immune lymphocytes were unable to bind and carry into culture sufficient antigen to allow for their subsequent activation. These results were not due to the induction of tolerance in the lymphocytes, since cultures of antigen-pulsed and untreated lymphocytes were equally responsive to continuous PPD when macrophages were added to the cultures, even when the antigen-pulsed lymphocytes had been exposed to high concentrations of PPD for 1 or 24 hr. In contrast, macrophages which were incubated for 1 hr at 37°C with a given concentration of PPD were as effective as the same concentration of PPD present continuously in macrophage-lymphocyte cultures in the induction of a lymphoproliferative response. Macrophages appear to play an obligatory role in the presentation of antigen to the immunospecific thymus-derived (T)-lymphocyte.
Restricted Clonal Response to DNP in Adult Offspring of Immunized Mice: A Maternal Effect
Authors: Kindred Berenice , Roelants Georges E. 
Published: December 2022

Abstract
Preoccupation with the status of a fetus as a homograft within the mother seems to have led to a virtual overlooking of the mother as the environment of the fetus. The problem of the possible effect on the young of immunization of the mother was studied by comparing adult offspring obtained before and after maternal immunization in their response to nitrophenyl haptens. Maternal immunization has a strong influence on the response to nitrophenyl haptens of subsequently conceived offspring. They show, compared to young obtained before maternal immunization, a more restricted anti-DNP response both in terms of circulating antibody titer, determined by a modified Farr assay, and of the number of DNP-specific clones expressed, determined by isoelectric focusing.
Possible mechanisms for this “maternal effect” and its relevance to studies of families showing antibodies of restricted isoelectric-focuing patterns are discussed.