bluuebunny/crossref_metadata_2025_split huggingface dataset:
Purification of the First Component of Human Complement by Affinity Chromatography on Human γ Globulin Linked to Sepharose
Authors: Bing David H. 
Published: December 2022

Abstract
The first component of human complement, C1̄, has been purified by affinity chromatography on a resin consisting of Sepharose covalently linked to human IgG. This resin selectively adsorbs at least 90% of the C1̄ detectable in a precipitate of human serum prepared at a final ionic strength of 0.03 and pH of 6.4. The C1̄ is eluted from the resin with 0.2 M 1, 4-diaminobutane. Virtually all the protein is recovered and the C1̄ has a high specific activity whether assayed with N-carbobenzoxy-L-Tyrosine-para-nitrophenyl ester or with EAC4, C2 and C-EDTA. Evidence that the protein obtained by this procedure is indeed C1̄ is based on the ability of C1̄ inhibitor to inhibit the enzymatic activity, of anti-C1s̄ antiserum to inhibit EAC4̄,2̄ formation and of the eluted protein to form the EAC1̄,4 intermediate. The procedure appears to be a simple reliable technique for preparing large quantities of human C1̄.
Bone Marrow-Derived Cells as Target Cells for Polynucleotide Adjuvants
Authors: Campbell P. A. , Kind P. 
Published: December 2022

Abstract
Mice were immunized with 107 sheep red blood cells (SRBC), with or without polyadenylic and polyuridylic acid adjuvant. Kinetics of the number of plaque-forming cells and cell units that could form hemolytic foci in recipient mice were studied. The adjuvant enhanced the number of plaque-forming cells on days 2 through 4 of the response but did not increase the number of hemolytic focus-forming units at any time. Since the limiting cell for the formation of hemolytic foci is probably the thymusderived cell, the adjuvant does not appear to act on cells of this type. The adjuvant appears to enhance the plaque-forming cell response at the level of the bone-marrow cell by a) increasing mitosis of bone marrow-derived cells, and/or b) by increasing the number of bone marrow-derived cells that interacted with thymus-derived cells.
Immunoglobulin E Antibodies in Guinea Pigs: Characterization of Monomeric and Polymeric Components
Authors: Dobson Colin , Rockey John H. , Soulsby E. J. L. 
Published: December 2022

Abstract
Immunization of Hartley strain guinea pigs with large doses (1 to 5 mg) of an ethylchloroformate polymerized Ascaris suum antigen, and immunization subsequently followed by infection with living second-stage larvae of the parasite, resulted in the production of both IgE (γE) and IgG1 (γG1) homocytotropic antibodies in high titer. Reaginic (PK) activity was assayed after a 6-day latent period and sedimented in sucrose density gradients at 8.3 ± 0.3S and 10.7 ± 0.3S. Both the 8S and 11S components were also demonstrated by antiglobulin enhancement of hemagglutination with specific anti-guinea pig IgE and anti-human IgE sera. The 11S reaginic antibody had a greater skin-sensitizing activity than the 8S component on the basis of the relative quantities detected following antiglobulin enhancement. The reaginic activity also was separated into different sized components by Sephadex G-200 gel filtration. Guinea pig PK activity was not absorbed by rabbit anti-guinea pig IgM (γM) or anti-IgG2/G1 (γG2/G1) sera. The IgG1 (γG1) (passive cutaneous anaphylatic (PCA) activity, assayed after an 18-hr latent period, was removed by the anti-IgG2/G1 (γG2/G1) serum. Reaginic activity was absorbed by rabbit anti-guinea pig IgE (γE) sera, and also by monospecific anti-human IgE (myeloma PS) serum. The anti-guinea pig IgE and anti-human IgE sera did not absorb guinea pig IgG1 PCA activity. Both monomeric and polymeric reaginic activities were absorbed by rabbit anti-guinea pig IgE serum. These experiments establish that guinea pig reaginic (IgE (γE)) antibody is the analogue of human reaginic antibody of the IgE class, and that the guinea pig and human IgE-globulins share common class-specific antigenic determinants.
The Relationship of Complement Consumption to Immune Fever
Authors: Mickenberg Ira D. , Snyderman Ralph , Root Richard K. , Mergenhagen Stephen E. , Wolff Sheldon M. 
Published: December 2022

Abstract
The administration of cobra venom factor or soluble human serum albumin (HSA)-anti-HSA complexes in antigen excess to rabbits resulted in a lowering of total hemolytic complement and C3 titers which persisted more than 24 hr. When such animals were challenged with complexes made up in 10 times antigen excess, the consumption of complement, febrile and thrombocytopenic responses were significantly diminished from those seen in untreated controls, and the duration of post-challenge leukopenia was shortened. These observations suggest a role for complement consumption, particularly of components C3-9, in the manifestation of these responses. Pyrogenic tolerance to complexes could not be explained by their more rapid removal from the circulation or a failure of the thermoregulatory centers to respond to preformed leukocytic pyrogen, suggesting that impairment in complement consumption either by depletion of C3 or interference with the activation of C1 might be responsible for this state. In contrast to these findings using complexes in 10 times antigen excess, similar prior treatment of immunized rabbits given HSA or of normal rabbits that received a mixture of soluble and insoluble complexes in 3 times antibody excess failed to suppress febrile or hematologic responses. If the formation of antigen-antibody complexes is essential for the production of these responses in immunized animals challenged with specific antigen, it appears that the large, rapidly-cleared complexes formed near equivalence are most likely involved in producing these biologic activities. Whereas some of the properties of these complexes make them more able to fix complement in vitro, it seems unlikely that complement-mediated mechanisms are significantly involved in the pathogenesis of the in vivo responses measured in these investigations.
Membrane Immunoglobulins of Lymphocytes in NZB Mice
Authors: Bhoopalam Nirmala , Yakulis Vincent J. , Costea Nicolas , Heller Paul 
Published: December 2022

Abstract
Mammalian lymphocytes of spleen, marrow, lymph nodes and peripheral blood have been found to have membrane sites with the structural characteristics of immunoglobulin which have been considered to be receptors for antigens and appear to be indicative of the capacity of these cells to synthesize immunoglobulins (1–7). We have recently found (8) that the proportion of these receptor-carrying lymphocytes (RCL) diminishes in BALB/c mice during the development of plasmacytoma. We were interested to determine if there was also a diminution in the percentage of RCL in other diseases associated with immunologic deficiency, e.g., in NZB mice during the development of the characteristic autoimmune disease.
NZB and CF1 mice were divided into three groups according to age: older than 6 months, less than 3 months, and a small group of newborns. Old mice of the BALB/c, SWR and C57B1 strains were also studied. Heparinized blood was obtained from each mouse by puncture of the retro-orbital venous sinus.
The Immunologic Release of Constituents from Neutrophil Leukocytes
Authors: Henson Peter M. 
Published: December 2022

Abstract
The reaction of rabbit neutrophils with immune complexes induced release of constituents to the external medium. The release which accompanied adherence of neutrophils to immune complexes bound to a nonphagocytosable surface resulted from a direct extrusion of granules to the exterior of the cell. Alkaline phosphatase from the secondary granule was released before constituents of the primary granule and remained at the site of excretion, adherent to the external neutrophil membrane.
In contrast, while phagocytosis of particulate complexes stimulated release of materials from the primary granules, alkaline phosphatase was released in only small amounts. A possible mechanism of enzyme release during phagocytosis of large particles was demonstrated to occur by two steps. Degranulation into the phagocytic vacuole was followed by opening of the vacuole during uptake of additional particles. Neutrophils were not lysed during either release process.
Anthrax Indirect Microhemagglutination Test
Authors: Buchanan Thomas M. , Feeley James C. , Hayes Peggy S. , Brachman Philip S. 
Published: December 2022

Abstract
A new application of the indirect microhemagglutination (IMH) test has been developed for anthrax. The antigen was prepared by DEAE cellulose, Dowex 1-X1, and Sephadex G-50 column chromatography of a culture filtrate of the avirulent, non-proteolytic, non-encapsulated Vollum strain of Bacillus anthracis grown anaerobically in a chemically defined liquid medium. Tanned, sensitized sheep red blood cells (SRBC) were tested with complement-inactivated SRBC-absorbed serum samples from 72 anthrax patients, 91 persons who had been vaccinated against anthrax, and 103 controls. The IMH test detected antibodies in 93% of patients, 98% of vaccinees, and none of the controls. Run-to-run reproducibility was 76% within one twofold dilution, and 93% within two twofold dilutions. The IMH test proved more sensitive and less time-consuming than the currently used agar-gel precipitation inhibition (AGPI) test.
Immunoglobulins in Intact, Immunized, and Contaminated Axenic Mice: Study of Serum IgA
Authors: Benveniste J. , Lespinats G. , Adam C. , Salomon J.-C. 
Published: December 2022

Abstract
The study of immunoglobulin levels of intact, immunized and/or contaminated axenic mice showed that: 1) axenic mice had lower levels of serum IgG2 and IgG1 than did holoxenic mice, but both immunoglobulin levels rose sharply after immunization or contamination of the former. In contrast, serum IgA remained undetectable in axenic mice after immunization and at 21 days after contamination; 2) serum IgA appeared about 2 months after massive contamination of axenic mice or 6 days after administration of prednisolone to them. The effect of prednisolone on serum IgA seemed to be related to passage of IgA from the intestinal system into the blood without true activation of the serum system.
Isolation of the Anticomplementary Protein from Cobra Venom and its Mode of Action on C3
Authors: Müller-Eberhard Hans J. , Fjellström Karl-Erik 
Published: December 2022

Abstract
Cobra factor, a protein of the venom of Naja naja, was isolated. It was characterized as a glycoprotein with a molecular weight of 144,000 and an electrophoretic mobility of a β globulin at pH 8.6. Added to whole human serum it converted and inactivated C3. The effect on C3 was found to be dependent upon a non-complement plasma protein and on bivalent cations. To generate C3-directed enzymatic activity, cobra factor had to enter into a firm complex with the plasma protein, a 5S thermolabile β pseudoglobulin.
Antibody Against Neoplastic Plasma Cells
Authors: Watanabe Takeshi , Yagi Yasuo , Pressman David 
Published: December 2022

Abstract
Rabbit antisera against cellular components of BALB/c mouse myeloma were found to contain antibodies which are specific for surface antigens present on both normal and neoplastic plasma cells. When spleen cells from mice previously immunized with sheep erythrocytes were exposed to the antisera and rabbit complement prior to assay, the formation of hemolytic plaques was strongly suppressed, even though the viability of spleen cells in general was not affected. The suppressive effects of anti-myeloma sera on direct and indirect plaque-forming cells (PFC) were similar in both primary and secondary responses. The suppressive effect was seen with PFC of all the inbred strains of mice tested. The surface antigens which react with the PFC-suppressive antibodies are also present on myeloma cells, but do not appear to be present in any significant amounts on lymphocytes of thymus, lymph node and spleen, or on cells of liver and kidney.
Immune Adherence Reactions of Human Erythrocytes Sensitized with Complement In Vitro and In Vivo
Authors: Petz Lawrence , Fudenberg H. Hugh , Fink Diane 
Published: December 2022

Abstract
Human erythrocytes and erythrocyte stroma sensitized in vitro with antibody and complement are reactive in immune adherence (I.A.). This was demonstrated by using isoantibodies (anti-A, anti-Lea) and with autoantibodies obtained from patients with the cold hemagglutinin syndrome or paroxysmal cold hemoglobinuria (P.C.H.). Although trypsin destroys the I.A. receptor site on human erythrocytes used as indicator particles, it did not diminish the ability of the cells to fix complement and participate in I.A. as the antigen-antibody-complement complex. Erythrocytes from patients with warm antibody autoimmune hemolytic anemia (A.I.H.A.), the cold hemagglutinin syndrome, or P.C.H., which were strongly sensitized in vivo with C3 as judged by agglutination tests (and stroma prepared from such erythrocytes), were uniformly negative in I.A., indicating a lack of biologic reactivity of cell-bound C3 in these disease states. Paroxysmal nocturnal hemoglobinuria (P.N.H.) erythrocytes lysed by fresh acidified normal human serum were negative in I.A., in striking contrast to positive results obtained with the same concentration of stroma of erythrocytes sensitized with complement by isoantibodies or autoantibodies. Erythrocytes that had fixed C3 by mechanisms possibly of a nonimmunologic nature were negative in I.A. Although quantitative factors may be the explanation for negative immune adherence in some of these test systems, qualitatively different C3 fixation may also account for such findings. The I.A. receptor site on human erythrocytes was shown to be present on P.N.H. erythrocytes and umbilical cord erythrocytes and was not inhibited by sensitization with a variety of isoantibodies or penicillin. However, the erythrocytes of one of 13 patients with warm antibody A.I.H.A. gave negative results when used as indicator particles, and the autoantibody in this patient's serum inhibited the I.A. receptor site of normal erythrocytes.
Potentiation of Cultured Mouse Thymocyte Responses by Factors Released by Peripheral Leucocytes
Authors: Gery I. , Gershon R. K. , Waksman B. H. 
Published: December 2022

Abstract
Lymphoid cell interactions in the immune response, both in vivo and in vitro, have been the subject of much interest recently (1, 2). In this regard, substances have been found in supernatants of cell cultures which can affect the response of other lymphoid cells (3, 4). The following report describes a new effect wherein mouse thymocytes are highly stimulated by a combination of nonspecific stimulants and substances released by human leucocytes.
Five × 106 thymus or spleen cells from male CBA/H or CBA/J mice, aged 6 to 12 weeks, were cultured in duplicate in plastic tubes (Falcon #2001) in 1.0 ml MEM-S (Microbiological Associates, Bethesda, Md., with added antibiotics and l-glutamine), supplemented with 8% normal human serum. These cultures were stimulated by the following, added singly or in combination: a) 1.0 µl phytohemagglutinin-P (PHA, Difco Laboratories, Detroit, Mich.); b) different concentrations of human white blood cells (obtained by gravitational sedimentation of the erythrocytes); c) supernatants (SUP) from cultures of human leucocytes.
Amino Terminal Sequences of Heavy and Light Chains of Chicken Anti-Dinitrophenyl Antibody
Authors: Kubo Ralph T. , Rosenblum Irwin Y. , Benedict Albert A. 
Published: December 2022

Abstract
Based on their amino terminal sequences human κ and λ light (L) chains form several subgroups (1–3). The L chains of the immunoglobulins of other animal species have been classified as homologues of the κ and/or λ classes (4). The κ class has been characterized as having a free (unblocked) amino terminus and a carboxyl terminal half cystine residue, whereas the λ class has been considered generally to have a blocked amino terminus, usually pyrrolidone carboxylic acid, and a penultimate half cystine residue at the carboxyl terminus (4, 5). Based on these criteria, Hood et al. (4) suggested that the chicken L chain was a κ type. Although the L chain from normal chicken IgG has an unblocked N-terminal amino acid (4, 6), we reported that the first 17 residues appeared to fit better in the N-terminal sequence of human λ rather than κ chains (6).
Functional Heterogeneity of Murine Lymphoid Cells
Authors: Stobo John D. , Rosenthal Alan S. , Paul William E. 
Published: December 2022

Abstract
Concanavalin A is a potent stimulant of in vitro blast transformation and of DNA synthesis by murine lymphoid cells. In contradistinction to phytohemagglutin which stimulates thymocytes minimally, concanavalin A causes marked responses on the part of both thymus cells and spleen cells. Both of these stimulants lead to meager responses on the part of bone marrow cells.
In the spleen and the bone marrow, the cells responsive to both agents appear to be thymus derived or thymus dependent. Thus, treatment of bone marrow cells with complement (C) and iso-antisera directed against the thymus dependent differentiation antigen ϑ abolishes the Con A and phytohemagglutinin (PHA) responsiveness of these cells. Spleen cells from adult mice which have been thymectomized, irradiated and reconstituted with bone marrow cells exhibit depressed responses to Con A and are unresponsive to PHA. Treatment of these cells with anti-ϑ antisera and C abolishes their residual Con A responsiveness.
Despite differences in the reactivity in various lymphoid cell populations to Con A and to PHA, similar amounts of radioiodinated mitogen can be bound to the surface of these cells. Thus, the number of Con A molecules which can bind to the highly responsive spleen and thymus cell populations is similar (∼10 × 106) to that which binds to the weakly reactive bone marrow cells. Spleen cells from thymus-deprived mice bind similar amounts of Con A and PHA as do spleen cells from intact mice. Among given lymphoid cell populations, a heterogeneity in Con A binding can be demonstrated either by fractionation of the population on Con A-polyacrylamide affinity columns or by direct light and electron microscopic visualization using covalent complexes of Con A with horseradish peroxidase or with ferritin.
An estimate of the number of Con A molecules which are required to bind to a cell surface to yield maximal stimulation was obtained by presensitizing thymus and spleen cells at 4°C with varying concentrations of Con A. Binding of approximately 1.5 to 2.5 × 106 molecules to these cells yielded optimal stimulation.
These results are discussed in terms of heterogeneity of mouse lymphoid cell populations and of the complex requirements for cellular stimulation by mitogen.
A Study of Tumor Allograft Sensitized Lymph Nodes in Mice
Authors: Irvin George L. , Eustace John C. , McAleer James A. , Levi Donald F. 
Published: December 2022

Abstract
The immunoglobulin synthesis by immune lymph node cells, which in vivo have been shown to transfer adoptively accelerated tumor allograft rejection and enhancement, was studied by in vitro techniques. Autoradiographs of tissue culture supernatants showed that lymph node cells that were sensitized for 5 days and were capable of mediating rejection immunity were producing peak amounts of IgM and increased amounts of 7Sγ2, but there was no increase in 7Sγ1 immunoglobulin when compared to unsensitized nodes. The autoradiographs of lymph node cells sensitized for 14 days, which in vivo transferred enhancement activity, showed that these cells synthesized maximal amounts of 7Sγ2 and 7Sγ1 immunoglobulins, but decreased amounts of IgM when compared to 5-day immune cells. There were no consistent differences in the synthesis of IgA by normal or immune lymph node cells. Fluorescent antibody studies confirmed the results of the tissue culture experiments and extended these findings by localizing the site of immunoglobulin production within the node to the hilar and medullary cord areas. While antisera specific for all immunoglobulin classes stained the mature germinal centers of 14-day nodes, the quality of the staining reaction suggested entrapment of immunoglobulin in these cortical areas rather than active synthesis. Concomitant with the development of transferable biologic activities and immunoglobulin synthesis by the allograft sensitized lymph node cells was the appearance of many large, immature blastoid cells within the node. A correlation of immunoglobulin synthesis by immune lymph node cells in vitro with accelerated rejection immunity and enhancement activity mediated in vivo is presented.
Naturally-Occurring Antibodies to Bacillary Teichoic Acids
Authors: Decker Gene P. , Chorpenning Frank W. , Frederick G. Thomas 
Published: December 2022

Abstract
Extracts from two Bacillus species were purified and characterized chemically as glycerol teichoic acids. Although neither alanine nor other amino acids were present, the purified substances adsorbed spontaneously to erythrocytes, as demonstrated by passive hemagglutination with antisera to bacilli and to the purified substance. The antibodies reacting in passive hemagglutination and precipitation tests were the same and the specificity was directed toward polyglycerophosphate. Purified antigens from the two Bacillus species exhibited a single band of identity in immunodiffusion tests. Antibodies to this glycerol teichoic acid occur regularly in several animal species, including man. They were not found in albino mice. In humans and guinea pigs, these antibodies were observed in both IgM and IgG Sephadex fractions but in rabbits they were usually found only in the IgM fraction.
Alteration in Graft vs Host Reactivity and in Hematopoietic Stem Cells of Spleen Cell Inocula from Donor Mice Pretreated with Pertussis Antigen
Authors: Eikman Edward A. , Bowser Robert T. 
Published: December 2022

Abstract
The graft versus host reactivity (GVHR) and hematopoietic stem cells of spleen cell inocula were assayed 3 days after pretreatment of donor mice with heated or unheated pertussis vaccine. Unheated vaccine reduced GVHR to 17% of control reactivity, measured by the Simonsen spleen weight assay, and increased 2.2-fold the proportion of hematopoietic stem cells, assayed as colony forming units (CFU). Heated vaccine, which did not produce the lymphocytosis induced in donors by unheated vaccine, reduced GVHR to 38% of control reactivity, and increased the proportion of CFU 3.8-fold. Alternative mechanisms for these effects are discussed.
Genetic and Cellular Factors in the Immune Response
Authors: Sloan Bruce P. , Gill Thomas J. 
Published: December 2022

Abstract
Immunization with an aggregated antigen decreased the antibody response in the highly responding ACI strain and enhanced the antibody response in the poorly responding F344 strain; the effects occurred with a variety of aggregating agents. These findings are consistent with the hypothesis that a major factor in the action of the aggregate is the prolonged retention and slow release of the antigen. There were more differences in the distribution of antibodies among chromatographic subclasses in the F344 strain than in the ACI strain, and these differences did not always correlate with the net charge of the antigen. Most of the differences in the F344 strain were in the antibodies eluting with 0.01 M buffer (IgG2), whereas the differences in the ACI strain were almost entirely in the antibody eluting with 0.20 M buffer (mainly IgG1). Aggregating the antigen caused some differences in the chromatographic subclasses of the antibody compared to those elicited by the antigen alone, and the differences were also strain-dependent.
The highly responding ACI strain mounted a strong delayed hypersensitivity response against both free and aggregated poly(Glu52Lys33Tyr15), whereas the poorly responding F344 strain was sensitized only by the aggregated polypeptide. Immunization with DNP-poly(Glu52Lys33Tyr15) aggregated with MeBSA or with polylysine sensitized the animals to the antigen and the aggregating agent, but not the hapten.