bluuebunny/crossref_metadata_2025_split huggingface dataset:
Specifically Cytotoxic Lymphocytes Produced by Preincubation with Antibody-Complexed Target Cells
Authors: Perlmann Peter , Perlmann Hedvig , Biberfeld Peter 
Published: December 2022

Summary
Highly purified human blood lymphocytes which had been incubated with antibody-complexed chicken erythrocytes, adsorbed 50 to 100 × more of this antibody (rabbit) than lymphocytes incubated with antibody-IgG without erythrocytes. Most of the adsorbed IgG was present in the form of antigen-antibody complexes, derived from lysed erythrocytes and not removable from the lymphocytes by repeated washing. When tested in subsequent cytotoxicity tests, the lymphocytes which carried antigen-antibody complexes were specifically cytotoxic for freshly added chicken erythrocytes. This was not the case with lymphocytes preincubated with antibody-IgG alone, with antibody IgG and noncross-reactive duck erythrocytes, or with IgG from normal rabbit serum. The results indicate that some lymphocytes have high affinity for antigen-antibody complexes. Antibody taken up in this way may be reutilized, thereby conferring specific effector functions on a population of normal lymphocytes. When complex-carrying lymphocytes were incubated with fresh erythrocytes and small amounts of fresh anti-erythrocyte antibody, however, they were less cytotoxic than those preincubated with antibody alone or with normal rabbit IgG. This may at least in part reflect a competition for lymphocytic sites with affinity for immunoglobulin and may be necessary for triggering of the antibody-induced cytotoxicity of lymphocytes.
The IgA System of the Guinea Pig
Authors: Vaerman J. P. , Heremans J. F. 
Published: December 2022

Abstract
The existence of the IgA system of the guinea pig has been established on the following grounds. 1) An 11S immunoglobulin (guinea pig IgA) has been isolated from milk and has been found to differ from IgM, IgG1 and IgG2. 2) An antiserum against this protein contained antibodies capable of eliciting the classical spur of secretory IgA over serum IgA, enabling to identify both the bound and free form of the secretory component. 3) IgA is a minor immunoglobulin constituent of guinea pig serum but a major immunoglobulin in secretions. 4) The electric charge and molecular size properties (large amounts of dimer) of guinea pig serum IgA were those characteristic for this immunoglobulin in other mammalian sera. 5) The majority of the immunoglobulin-containing cells of the intestinal mucosae of the guinea pig produce IgA, in contrast to IgM and IgG which is mainly found in the immunocytes of the spleen and lymph nodes.
Induction of Cross-Tolerance for Contact Sensitivity by a Non-Immunogenic Chemical
Authors: Baer Rudolf L. , Rosenthal Stanley A. 
Published: December 2022

Abstract
1,2-dichloro-4-nitrobenzene (DcNB), a non-immunogenic chemical, when fed to guinea pigs 21 days before attempted contact sensitization to 2,4-dinitro-1-chlorobenzene (DNCB), induced tolerance with respect to contact sensitivity to DNCB. The tolerance was specific since DCNB induced no tolerance to citraconic anhydride under similar experimental conditions. Guinea pigs which were contact sensitive to DNCB did not cross-react to DCNB. The theoretical and potential practical implications of these findings are discussed.
Effect of Carrier Modification on the Cellular and Serologic Responses of the Rat to the Tnp Hapten
Authors: Hirsh Dwight C. , Amkraut Alfred A. , Steward John P. 
Published: December 2022

Abstract
Soluble trinitrophenylated keyhole limpet hemocyanin (s-TKLH) was made particulate by reacting with ethyl chloroformate. After i.p. injection, the anti-hapten response was measured by passive hemagglutination and by plaque-forming cells (PFC) in the parathymic lymph nodes (PLN) and spleen. Titers were higher, and the slopes of the log phase were dose-independent for particulate TKLH; titers were lower, and the slopes of the log phase were dose-dependent for soluble TKLH. The peak number of 7S PFC in the PLN was sustained with particulate TKLH, but decreased rapidly with soluble TKLH. The number of PFC in the spleen was not above background. The priming ability of particulate antigen was 10 to 100 times that of soluble antigen in the PLN, other lymph nodes and spleen.
Particulate TKLH was phagocytosed by macrophages 20 to 30 times more efficiently than was soluble TKLH. Association with macrophages, however, enhanced the immunogenicity of soluble TKLH greatly, while it almost abolished the primary response to particulate TKLH, and significantly reduced the secondary response. Furthermore, antigen-containing granulomata found in the peritoneal cavity 3 days after injection of the particulate antigen did not induce an immune response when transplanted to normal rats. We concluded that increased uptake or differential processing by peritoneal macrophages does not account for the greater immunogenicity of particulate TKLH.
Retention of particulate TKLH in the liver and spleen was much greater than that of soluble TKLH, and may account for some, but not all, of the differences we report. Possible suppressive effects of excess soluble antigen will be discussed in a subsequent paper.
Inhibition of Phytohemagglutinin-Induced Lymphocyte Transformation by α Globulins; Lack of Correlation with Phytohemagglutinin Precipitation by Serum Proteins
Authors: Yachnin Stanley 
Published: December 2022

Summary
Human α globulin will suppress the in vitro transformation of human lymphocytes induced by two highly purified mitogens isolated from crude phytohemagglutinin preparations. Only one of the mitogen preparations (H-PHAP), however, forms nonspecific precipitates with human serum or isolated α globulin preparations. These results suggest that α globulin does not interfere with phytohemagglutinin-induced transformation by virtue of a direct reaction with the reaction with the mitogen.
The Early Stimulation of Protein Synthesis in Sensitized Guinea Pig Lymph Node Cells by Antigen
Authors: Levy Ronald , Rosenberg Steven A. 
Published: December 2022

Abstract
Lymph node cells from immunized guinea pigs were studied in short-term cell culture to determine the effect of specific antigen on protein and RNA synthesis. Both RNA and protein synthesis were stimulated early after the addition of antigen to these cultures. Pulse-labeling techniques disclosed a stimulatory effect on protein synthesis by antigen as early as 4 hr after its addition. This stimulatory effect was associated with the specific release of a soluble non-dialyzable mediator which recruited nonsensitized cells to increase their rate of protein synthesis. The stimulatory effect of antigen on protein synthesis was abolished by the prior addition of actinomycin D.
Detection of Serum-Hepatitis Antigen by Charcoal Particle Agglutination-Inhibition
Authors: Stevens Roy W. , Ziegler F. D. , Kelly James H. 
Published: December 2022

Abstract
A new method has been developed for the detection and quantitation of the antigen related to serum hepatitis. This antigen, in addition to its association with serum hepatitis (1, 2), has been implicated more recently in a variety of other disease states (3–5). The test reagent is serum-hepatitis (SH) antigen adsorbed to particulate charcoal. These particle-antigen complexes are macroscopically aggregated by homologous antisera and inhibition of this agglutination by a serum specimen forms the test for antigen. This communication describes the method and reports the findings of a serologic evaluation.
Materials and Methods. Serum-hepatitis antigen (lot 28-56-1) purified by zonal ultracentrifugation was obtained from Electro-Nucleonics Laboratories, Inc., Bethesda, Md. 20014. The antigen, after dialysis against 0.85% saline, was diluted and mixed with an aqueous suspension of fine charcoal particles (Hynson, Westcott, and Dunning, Inc., Baltimore, Md. 21201).
Immunoglobulin Content and Antibody Activity in Urine in Experimental Urinary Tract Infection
Authors: Smith James W. , Hand W. Lee 
Published: December 2022

Abstract
Immunoglobulin content and antibody content in urine were analyzed in rabbits following experimental urinary tract infection. IgA was present in urine from normal animals and in animals with urinary tract infection. Since it was present in urine whether it was synthesized locally or not, IgA in urine probably represents IgA excreted from serum. IgG was not present in urine from normal rabbits, but was present in urine from some animals with pyelonephritis. This IgG migrated as a fast component immunoelectrophoretically, had antibody activity, and had the capability of crossing renal and intestinal epithelium. This unique IgG probably represents IgG synthesized by a restricted population of cells within the infected kidney. IgG was present in urine from all animals with bladder infection and represents newly synthesized IgG which can cross the inflamed bladder mucosa.
Assay of IgG and Other Human Plasma Proteins by Quantitative Inhibition of Passive Hemagglutination
Authors: Nusbacher Jacob , Berkman Eugene M. , Wong Kwan Y. , Kochwa Shaul , Rosenfield Richard E. 
Published: December 2022

Abstract
Using tanned human red cells coated optimally with isolated plasma proteins, specific agglutination in an AutoAnalyzer was quantitatively inhibited by solutions of the coating protein. IgG, IgM, IgA, IgD, IgE, transferrin, fibrinogen and ceruloplasmin were assayed in this manner. Lowest detectable concentrations varied from 0.2 µg IgE/ml and 0.4 µg IgG/ml to 9 µg IgD/ml. The amount of 125I-labeled IgG bound by tanned cells was a linear function of the amount applied when both variables were treated as logarithms, and about 2000 bound molecules per cell were optimal for agglutination. IgG appeared to bind at its Fab region, but less than 5% of the lowest applied concentrations was bound. Assays of cerebrospinal fluid for IgG compared favorably with quantitative precipitin data, but some myeloma proteins were not assayed reliably in reference to normal IgG.
A Quantitative Method for Determining Human γG Allotype Antigens (Gm)
Authors: Litwin S. D. , Balaban S. 
Published: December 2022

Abstract
Quantitative measurements of human γG allotype antigens (Gm) provided information on some of the factors controlling the sera expression of immunoglobulin allotypes. The data suggested different rates of synthesis by allelic Gm genes at two γG subclass loci. This was apparent from the striking differences in the serum expression of antithetical γG3 allotypes, Gm(b) and Gm(g), and a smaller difference for the γG1 isoalleles, Gm(f) and Gm(a). In heterozygous sera, Gm(b+) γG constituted 70% of the γG3 heavy chains and Gm(g) 30%; Gm(f+) γG constituted 54% of γG1 chains and Gm(a) 46% (mean values). Allotype values were consistent with γG class and subclass measurements. A gene dosage effect was also present, reflected in the differences between mean values of homozygous and heterozygous subjects—although phenotype ranges overlapped.
The data indicated that normal heterozygous sera contained close to balanced proportions of each γG1 gene product. Certain exceptional hypergammaglobulinemic sera had unusual distributions of allelic γG1 heavy chains without evidence of a monoclonal component.
Characterization of the Surface Antigens of Staphylococcus Aureus, Strain K-93M
Authors: Karakawa Walter W. , Kane Judith A. 
Published: December 2022

Abstract
Three distinct surface antigens were isolated from the culture filtrate of Staphylococcus aureus, strain K-93M, by a combination of Cetavlon precipitation, ion-exchange chromatography, and gel-filtration. Chemical analysis indicated that the immunologically predominant constituent of the K-93M filtrate material was a glucosaminuronic acid-alanine complex which was chemically analogous to the Smith antigen, the capsule prototype of S. aureus. Immunochemical studies confirmed the structural relationship between the Smith capsule and the glucosaminuronic acid polymers isolated from the K-93M culture filtrate. Quantitative precipitin analysis suggested that glucosaminuronic acid is the immunodominant determinant of this antigen.
Chemical analyses indicated that the second acidic polymer was composed of mannose, galactose and phosphorus; whereas the third polymer was composed of galactose and galacturonic acid. Immunologic studies revealed that both of these polymers were also distinct antigenic polymers.
A Protein in Normal Nurse Shark Serum Which Reacts Specifically with Fructosans
Authors: Harisdangkul Valee , Kabat Elvin A. , McDonough Robert J. , Sigel M. Michael 
Published: December 2022

Abstract
A protein which specifically precipitates with the fructosans, levans and inulin, was found in most normal nurse shark sera. It could be specifically purified on insoluble immunoadsorbent columns by using Sephadex G-75 or levan gel. From quantitative precipitin and inhibition studies, the combining site was found to react specifically with the β-D-fructofuranosyl (2 → 1) β-D-fructofuranosyl and β-D-fructofuranosyl (2 → 6) α-D-glucopyranosyl residues. The best inhibitor was a tetrasaccharide, β-D-fructofuranosyl (2 → 1) β-D-fructofuranosyl (2 → 1) β-D-fructofuranosyl (2 → 6) D-glucose (3F1G). The protein was unrelated to shark IgM antigenically and appears not to be an immunoglobulin of the usual type. Binding of the protein with its specific ligands caused specific fluorescence quenching and the association constants for various mono- and oligosaccharides were measured. The calculated relative association constants from precipitin inhibition assays and from fluorescence quenching for various mono- and oligosaccharides agreed closely and the homogeneity of the combining site was indicated by both methods. The association constant (K0) for 3F1G was 3.7 × 104 1/M. Two other carbohydrate-reacting proteins were also found in normal nurse shark sera. One precipitated with perennial rye grass levan which contained 2 → 6 linked fructofuranosyl residues. The other was specific for dextran B1355-S-4, which contained a high percentage of α(1 → 3) linked glucopyranosyl residues.
Specificity of the in Vitro Binding of IgG and Rabbit Serum Albumin (RSA) to Rabbit Yolk Sac Membrane
Authors: Sonada Shunro , Schlamowitz Max 
Published: December 2022

Abstract
A method is described for the study of specificity of binding of IgG and rabbit serum albumin (RSA) to rabbit yolk sac membrane in vitro. Yolk sac membranes are fixed with formaldehyde, challenged with 125I-IgG or 125I-RSA and then subjected to elution of the labeled protein by unlabeled IgG, RSA or other eluents Consistent results are obtained when elution data are expressed in terms of “specific elutability,” i.e., the fraction of the total membrane-bound protein that is eluted. The recognition and binding of IgG and RSA by membranes and their elution are essentially specific. Further, the displacement of membrane-bound 125I-IgG, but not 125I-RSA, by crude glycopeptide fractions prepared from IgG illustrates the applicability of this in vitro system for investigating the structural moieties of macromolecules that confer specific recognition to the macromolecules.
An Improved Primary Response from Mouse Spleen Cells Cultured in Vivo in Diffusion Chambers
Authors: Goodman S. A. , Chen M. G. , Makinodan T. 
Published: December 2022

Abstract
The optimum conditions for the hemolytic plaque-forming cell response of mouse spleen cells to sheep red blood cells (SRBC) in Millipore diffusion chambers were determined because of the wide applicability of the technique as an in vivo but closed system for the study of the immune response. The effect of pretreatment of chamber recipients with x-rays or cyclophosphamide, as well as the effects of chamber volume, culture medium, chamber detoxification and sterilization techniques, were investigated. The improvement in response over that previously reported by this laboratory was attributed to larger chamber volume, chamber detoxification twice over a 24-hr period, culture medium supplemented with horse serum, and lethally irradiated or cyclophosphamide-treated recipient C31F1 mice. With the improved conditions the peak primary response of mouse spleen cells to SRBC (104 direct plaque-forming cells per 106 nucleated cells harvested) was almost 20-fold greater than that obtained in the cell transfer system and about 5-fold greater than the best response obtained both in vitro and in situ. The burst size was also significantly larger than that obtained in the other systems, and culturing efficiency was twofold greater than previously reported from this laboratory for the diffusion chamber technique. The improved technique was used to determine the response of mouse spleen cells to SRBC in both allogeneic (across H-2 and non-H-2 barriers) and xenogeneic hosts. The enhanced response obtained by the present method is attributed to increased culturing efficiency and burst size, but not increased efficiency of interaction of the cells initiating the response.
Tissue Localization of Two Populations of Human Lymphocytes Distinguished by Membrane Receptors
Authors: Silveira Nelson P. A. , Mendes Nelson F. , Tolnai Marina E. A. 
Published: December 2022

Abstract
Lymphocyte suspensions from man and primates show a high proportion of cells adhering to sheep erythrocytes (E) forming rosettes (1–3). The binding of E to lymphocytes is dependent on temperature and is probably not immunologic in nature because 20 to 40% of normal human peripheral blood lymphocytes form rosettes when incubated with E (1). It appears as if the lymphocytes which have receptors for E constitute a subpopulation of lymphoid cells which are thymus dependent or derived (T) since almost 100% of human thymocytes form this type of rosette (1).
A number of reports validate the use of certain membrane markers for the characterization of lymphocyte populations. Distinct markers for “T” and bone marrow-derived (“B”) type cells have been described on the membrane of mouse lymphocytes: the theta (θ) alloantigen (4–6), the receptors for a modified complement component (C3) (7–9) and the membrane-bound immunoglobulins (8, 10, 11).
Measurement of Mycoplasma Pneumoniae Mycoplasmacidal Antibody in Human Serum
Authors: Brunner Helmut , James Walter D. , Horswood Robert L. , Chanock Robert M. 
Published: December 2022

Abstract
Investigation of the conditions which affect the mycoplasmacidal action of antibody and complement upon Mycoplasma pneumoniae indicated the importance of a filtered suspension of predominantly single organisms, and an appropriate concentration of cations. The mycoplasmacidal effect of antibody and complement resembled the hemolytic reaction in that variation in concentration of either antibody or complement yielded an S-shaped curve. The antigens involved in the mycoplasmacidal reaction appeared to be the glycolipids of the organism which had previously been shown to be of major importance in the complement fixation and metabolism inhibition reactions. The standardized mycoplasmacidal antibody assay proved to be considerably more sensitive than the conventional assay systems for measurement of M. pneumoniae antibody in human serum.
The Production of Anti-Dnp Antibody in the Bullfrog, Rana Catesbiana
Authors: Rosenquist Grace L. , Hoffman Ronald Z. 
Published: December 2022

Abstract
Bullfrogs injected with dinitrophenyl keyhole limpet hemocyanin (DNP-KLH) in complete Freund's adjuvant produced precipitating anti-DNP antibody with characteristics different from that produced by frogs immunized against DNP-Salmonella in saline.
The antibody from animals injected with DNP-KLH sedimented as a 7S protein on sucrose density gradients and gave precipitin curves similar to the precipitin curve of mammalian 7S-IgG except for the lack of 100% precipitability of the antigen over most of the frog curve.
DNP-Salmonella induced antibody which sedimented as a macroglobulin and was distinguished from the light antibody induced by DNP-KLH by radioimmunoelectrophoresis. The precipitin curve for this immunoglobulin and the persistence of high titers 1 year after a single injection suggest that the immunoglobulin is IgM.
Studies of Non-Migrating, Long-Lived Lymphocytes in Rats
Authors: Miller John J. , Shortman Ken , Byrt Pauline 
Published: December 2022

Abstract
Rat lymph node lymphocytes were labeled by hind footpad injections of tritiated thymidine in the absence of an immune stimulus or after priming with a polymerized Salmonella flagellin. Fifty or more days later the rats were killed and the lymph node cells were fractionated on continuous albumin density gradients. The proportions of lymphocytes of lighter density (&lt; 1.07 g/cm3) were greater in primed than in unprimed nodes. The density distributions of the “long-lived” cells, i.e., those with persistent label, were identical to those of the total lymph node cell population. After challenge with either antigenically identical or different flagellins, the density distribution of the persistently labeled cells demonstrated relative loss of cells in the density range from 1.068 to 1.072 g/cm3 in comparison to the bulk of lymph node cells, but not in patterns distinct for the specificity of the antigens used for challenge. Comparison of the density distributions of long-lived lymphocytes with flagellinbinding cells and with cells transferring adoptive immune reactions revealed partial overlap with these cells from primed but not from unprimed lymph nodes.
Phylogeny of Immunoglobulin Structure and Function
Authors: Leslie Gerrie A. , Clem L. William 
Published: December 2022

Abstract
Three different sizes of immunoglobulins containing anti-dinitrophenyl activity were isolated from turtles immunized with dinitrophenyl bovine γ globulin. The sedimentation coefficients of the three immunoglobulins were ∼17S, 7.5S and 5.7S and their molecular weights were 850,000, 180,000 and 120,000, respectively. The 17S immunoglobulin was similar to IgM and was composed of five subunits each with a molecular weight of ∼170,000. The heavy and light chain molecular weights were 70,000 and 22,500, respectively. The 7.5S molecule had H chains of ∼67,500 and L chains. The 5.7S molecule had H chains of ∼35,000 and L chains. Partial reduction of the 5.7S molecule resulted in the formation of half molecules of ∼61,000. Antigenic analyses suggested that the 5.7S molecule may be a fragment of the 7.5S molecule. Neither the 7.5S H chains nor the 5.7S H chains cross-reacted with the 17S H chains. These findings are discussed in relationship with the phylogeny in immunoglobulin structure and function.
Inhibition by Anti-µ Chain Sera of the Cellular Transfer of Antibody and Immunoglobulin Synthesis in Mice
Authors: Herrod Henry G. , Warner Noel L. 
Published: December 2022

Abstract
Unprimed mouse spleen cells were incubated in vitro with various class specific rabbit anti-mouse immunoglobulin sera. Cells were washed and transferred into syngeneic or allotype congenic irradiated recipients. Syngeneic recipients were stimulated at the time of cell transfer with sheep erythrocytes (SRBC) and Brucella abortus. At 7 days their IgM response to SRBC and B. abortus was significantly depressed following pretreatment with anti-µ chain sera, but not with anti-γ chain sera. Congenic recipients were serially bled and levels of donor type IgG immunoglobulins were determined by allotype specific inhibition of precipitation assays. Marked suppression of the transfer of donor type IgG of all classes was obtained by pretreatment with anti-µ chain sera.