bluuebunny/crossref_metadata_2025_split huggingface dataset:
Local Transfer of Delayed Hypersensitivity by T Lymphocytes
Authors: Jaffer Adrian M. , Jones Gerald , Kasdon Earl J. , Schlossman Stuart F. 
Published: December 2022

Abstract
It is now well established that lymphocytes consist of two major subpopulations, thymus dependent (T)2 cells and thymus independent (B) cells (1). These populations may be distinguished by the presence of readily demonstrable surface immunoglobulin on B cells compared with T cells (2). Although cellular immune reactions, such as skin graft rejection, are known to be thymus dependent, there is no direct evidence that T cells mediate delayed skin reactions. This report describes the production of delayed skin reactions in guinea pigs by lymphocytes depleted of Ig-bearing (B) cells. An insoluble anti-Ig column was used to remove B cells (3) and the ability of the B-depleted cell population to mediate delayed hypersensitivity was assessed by a local transfer technique (4).
Antiserum to guinea pig Ig was raised in rabbits and purified antibody was prepared with the aid of an insoluble immunoabsorbent of guinea pig globulin covalently bound to Sepharose 4B (5).
Human Immunoglobulin A: Production of an Fc Fragment by an Enteric Microbial Proteolytic Enzyme
Authors: Mehta Satish K. , Plaut Andrew G. , Calvanico Nickolas J. , Tomasi Thomas B. 
Published: December 2022

Summary
An Fc fragment has been prepared in good yield by proteolytic cleavage of human secretory and serum myeloma IgA with an enzyme recovered from the human gastrointestinal tract. The naturally occurring enzyme is of microbial origin and its activity is metal dependent.
Comparative Chemical Study of α- and µ-Chains from a Single Patient (SC)
Authors: Seon B.-K. , Yagi Y. , Pressman D. 
Published: December 2022

Abstract
In a previous report (1), we have shown that an IgA(κ) and an IgM(κ) myeloma protein derived from the same patient (SC) shared individually specific determinants which were found in the Fab portion of the molecules. We have also shown by various criteria that the light chains of these two immunoglobulins are identical (2). In the present work, we have compared the N-terminal amino acid sequence of the variable portion of the heavy chain of the IgA molecule with that of the IgM molecule and have found them both to be Glp-Met-Gln-Leu, a sequence not previously reported, but close to the VH1 heavy chain subgroup sequence, Glp-Val-Gln-Leu. In addition, peptide maps of chymotryptic digests showed appreciable identity between substantial portions of the variable portions of the α and µ heavy chains.
Materials and Methods. IgA and IgM and the Fab fragments of IgA and IgM were prepared as described previously (1).
Independent Movement of IgD and IgM Molecules on the Surface of Individual Lymphocytes
Authors: Knapp W. , Bolhuis R. L. H. , Rádl J. , Hijmans W. 
Published: December 2022

Abstract
It is now generally accepted that immunoglobulins (Ig) on the membrane of lymphocytes are mobile in the plane of the membrane itself. The reaction of divalent antibodies with the Ig molecules, which were originally diffusely distributed, induces cross-linkage and aggregation of the Ig molecules. These aggregates are then actively transported to one pole of the cell where they form the so-called caps. This capping process is markedly inhibited in the cold and can be blocked by different drugs (1, 2).
We used this phenomenon for the investigation of Ig molecules of two different classes (IgM and IgD) on individual lymphocytes.
Materials and Methods. Cord blood lymphocytes from 20 healthy babies and peripheral lymphocytes from 20 adults were investigated for the presence of membrane-bound Ig in immunofluorescence. Lymphocytes were obtained by gradient centrifugation with the Isopaque Ficoll technique (3). Cells were tested for viability and stained in suspension.
Antinucleolar Antibodies in Human Sera
Authors: Pinnas Jacob L. , Northway James D. , Tan Eng M. 
Published: December 2022

Abstract
Antibodies to mammalian cell nucleoli occur spontaneously in certain autoimmune human diseases and have been demonstrated by immunofluorescence. In this study, nucleoli were isolated from fresh calf thymus and antinucleolar antibodies were used as reagents to identify a reactive nucleolar antigen. The antigen was a low molecular weight 4–6S RNA, and the precipitating activity of this antigen was destroyed by treatment with spleen phosphodiesterase. Sera were selected for this study because of predominance of nucleolar staining by immunofluorescence and were found to be from patients with scleroderma, Sjogren's syndrome, and undiagnosed illnesses manifesting Raynaud's phenomenon.
The Role of Humoral Factors in the Initiation of in Vitro Primary Immune Responses
Authors: Watson James 
Published: December 2022

Abstract
Immune responses in thymus derived (T) cell-depleted mouse spleen cultures were stimulated by the addition of either syngeneic T cells immunized with antigen, or allogeneic T cells reactive against precursor antibody-forming cells. Both require the presence of specific antigen in cultures. At low T cell concentrations, (&lt; 106), allogeneic T cells are more effective in stimulating immune responses than the syngeneic T cells, however, at higher cell numbers (&gt; 106), allogeneic T cells suppress the response. The stimulation of in vitro immune responses to heterologous erythrocyte antigens is mediated by nonspecific activity released from antigen-stimulated T cells in culture supernatants. Fractionation of culture supernatants prepared in serum-free media, by Sephadex G-100 chromatography, revealed the presence of three thymus cell-replacing factors (TRF). The fractionation profiles of supernatant activities prepared from syngeneic and allogeneic T cells were identical. TRF-I from both T cell sources has a molecular weight around 150,000, is labile to heat, periodate, and trypsin, and requires the presence of θ-positive cells for production in culture. TRF-I does not appear to be immunoglobulin in nature. TRF-II (m.w. 15,000 to 40,000), and TRF-III (m.w. &lt; 7000) do not require the presence of θ-positive cells for production in culture. Syngeneic and allogeneic T cells also released a factor (m.w. 10,000 to 20,000) that suppressed the induction of normal in vitro immune responses.
Mechanisms of Endotoxin Tolerance
Authors: Greisman Sheldon E. , Young Edward J. , DuBuy Bernard 
Published: December 2022

Abstract
Acclimatized rabbits were passively immunized with graded volumes of antisera against endotoxins from either smooth wild type Gram-negative bacteria possessing intact O-antigenic side chains, or rough mutants deficient in these O-antigens. The recipients were challenged with test doses of endotoxins that evoked fever within the sensitive dose-response range. Pyrogenic tolerance conferred with antisera to smooth endotoxins was consistently directed toward the O-specific antigen; minimal protection extended to endotoxins from heterologous Gram-negative bacterial species, or from homologous O-deficient rough mutant strains. In contrast, antisera to O-deficient rough mutant strains transferred significantly more effective protection against heterologous endotoxins. The level of such heterologous protection, however, was markedly less than the O-specific protection conveyed by the smooth anti-endotoxin sera.
The protective factors in antiserum to smooth endotoxin were separable by either pyrogen-free Sephadex G-200 columns or ammonium sulfate precipitation into 2-mercaptoethanol (2-ME) resistant and sensitive O-antibody-containing fractions. In the latter, 2-ME virtually abolished O-agglutinating, but not O-combining or protective activities. Both O-combining and protective activities could be reduced by absorption of antiserum with spleen cells but not with erythrocytes.
It is concluded that: 1) the humoral components of endotoxin tolerance are antibodies to both O-specific and common core antigens. Such antibodies are both IgM and IgG, protect by primary (binding) rather than secondary (agglutinating) activity, and are in part cytophilic; 2) the relative importance of O-specific and common core antibodies is dependent upon both the immunizing and test endotoxin preparations. Antisera to smooth endotoxins afford the highest levels of passive tolerance, but such protection is restricted primarily to the O-specific endotoxin. Antisera to rough O-deficient endotoxins provide less tolerance but afford the better approach to broad passive endotoxin protection; 3) the findings support the hypothesis that common core antigens are partially masked by the O-specific antigens in the endotoxin molecule.
The Reaction of Zymosan with the Properdin System in Normal and C4-Deficient Guinea Pig Serum
Authors: Brade Volker , Lee Gerald D. , Nicholson Anne , Shin Hyun S. , Mayer Manfred M. 
Published: December 2022

Abstract
On incubation with serum, zymosan (Z) combines with several serum components, collectively designated X, to form an intermediate, ZX, which is capable of activating the complement system by cleavage of components C3 and C5. We now report kinetic studies on the formation of ZX, as well as the reaction of this intermediate with purified C3 or C5, which indicate that the splitting of these complement components is mediated by two multi-unit enzyme complexes on the zymosan particles, one which acts on C3, and another which splits C5. These two enzymes share in common factor B of the properdin system, but differ in other respects. On extended incubation at 37°C they decay to a form designated ZXd by release of the factor B subunit. ZX can be regenerated from ZXd by treatment with factor B but this process is efficient only with respect to C5 cleavage, presumably because a subunit of the C3-cleaving enzyme, other than factor B, is also lost during decay at 37°C. The reaction of factor B with ZXd to yield ZX is believed to be enzymatic on the basis of its temperature-dependence and its kinetic behavior. Presumably, an enzyme on ZXd activates factor B, probably by cleavage, thus enabling it to combine with ZXd to form ZX. This process of activation and fixation of factor B is believed to be the final step in the complex series of reactions leading to formation of the C3- and C5- cleaving enzymes on zymosan particles. Evidence is also presented that the formation of these enzymes on zymosan proceeds much more rapidly in normal guinea pig serum than in C4-deficient serum, which indicates a marked accelerating effect of the early-acting complement components.
Evidence for a Macrophage-Mediated Effect of Poliovirus on the Lymphocyte Response to Phytohemagglutinin
Authors: Soontiëns F. J. C. J. , Van Der Veen J. 
Published: December 2022

Abstract
Poliovirus inhibits the response of human peripheral leukocytes to phytohemagglutinin (PHA). The inhibitory activity requires the presence of macrophages. There is no evidence that lymphocytes are capable of supporting viral replication. On the other hand, the virus multiplies in macrophages derived from monocytes. Further, macrophages enhance the response of lymphocytes to PHA, but the cooperation between these cell types is absent in virus-infected cultures. The findings support the suggestion that poliovirus inhibits the response of leukocytes not by direct action on lymphocytes but by suppressing the enhancing effect of the macrophage.
Lymphocyte-Derived Eosinophil Chemotactic Factor
Authors: Torisu Motomichi , Yoshida Takeshi , Ward Peter A. , Cohen Stanley 
Published: December 2022

Abstract
When cultured in the presence of specific antigen, lymphocytes from delayed hypersensitive guinea pigs release a precursor substance (ECFp) which can be activated by specific immune complexes to yield an eosinophil chemotactic factor (ECF). The generation of ECFp like that of migration inhibition factor (MIF) is carrier specific. The immune complexes which activate ECFp must contain IgG2 antibody with specificity directed against the antigen which was used to stimulate the lymphocytes to produce ECFp. Previous studies have shown that this reaction does not involve complement.
It was not possible to dissociate MIF activity from ECFp activity by a combination of sephadex chromotography and agarose block electrophoresis. However, columns containing sepharose beads conjugated with specific antibody removed ECFp but not MIF from the supernatant fluids. Antigen-conjugated columns did not affect either activity. If the supernatants were activated with immune complexes before passage through the columns, then eosinophil activity could not be removed by either column. These results all suggest that ECFp co-precipitates with immune complexes by virtue of an antigenic fragment it contains. The activation of ECFp to ECF involves loss of this fragment.
A Mathematical Model for the Quantitation of Tumor and Antibody-Forming Cell Populations within an Animal's Body
Authors: Hiramoto Raymond N. , Ghanta Vithal K. , McGhee Jerry R. , Hamlin N. Marlene 
Published: December 2022

Abstract
The application of a mathematical model described by Hege and Cole was tested by a murine myeloma model. The plasmacytoma MOPC 104E secretes an IgM antibody to bacterial dextran B-1355. By using this system the various parameters required in the equation could be quantitated. The model relates the number of tumor cells in the population to antibody produced under conditions of logarithmic growth. Experimental values of antibody measured and estimation of starting population (An) of tumor cells showed that 2.24 × 106 cells grew when 3 × 106 cells were injected. This indicates that approximately 75% of the cells grew when 3.0 × 106 tumor cells were given i.p. into each mouse. The experimentally determined antibody levels were in agreement with the computer calculated values.
Hemolysis of Sheep Erythrocytes in Guinea Pig Serum Deficient in the Fourth Component of Complement
Authors: May Joseph E. , Frank Michael M. 
Published: December 2022

Abstract
Sheep erythrocytes sensitized with 20 to 40 times the quantity of IgG or IgM antibody required for lysis via the classical complement pathway undergo lysis in C4-deficient guinea pig serum (C4D) or C2-deficient human serum (C2D). The mechanism of this lysis was analyzed in detail, and was found to have an absolute requirement for a Cl-like protein and components of the alternate complement pathway.
Three independent lines of investigation suggested the requirement of C1 for lysis in the deficient sera: 1) C4D serum depleted of C1 by low ionic strength precipitation sustained a marked loss of lytic activity which was overcome by the use of the complement-cell intermediate EAC1. 2) C2D serum depleted of C1 by use of a monospecific anti-C1q immunoabsorbent sustained marked loss of hemolytic activity. Addition of properdin to such sera did not restore hemolytic activity. These absorbed sera were able to lyse the cellular intermediate EAC1. 3) Mg-EGTA completely inhibited lysis in C2D and C4D serum by this pathway while allowing normal function of the alternate complement pathway. Function of C4 and C2 in this lytic mechanism was further excluded by the absence of C2 consumption in C4D serum incubated with heavily sensitized RBC, the failure of anti-C4 to inhibit the lytic reaction, and the inability to lyse heavily sensitized RBC by the sequential addition of purified C1, C2, and C EDTA. Participation of components of the alternate complement pathway was suggested by: 1) conversion of the C3 proactivator by heavily sensitized RBC, 2) abolition or marked reduction of the cytotoxic capacity of C4D and C2D serum heated at 50°C for 30 min, conditions which did not deplete C1, and 3) abolition of lysis in C4D or C2D treated with 0.03 M hydrazine. This lytic mechanism utilizes the later acting complement components as shown by complete absence of lysis in rabbit serum lacking C6.
Recombination of the Polypeptide Chains of a Waldenström's IgM That Binds IgG
Authors: Schrohenloher Ralph E. , Mestecky Jiri 
Published: December 2022

Abstract
An IgM protein that reacted with human IgG was isolated from the plasma of a patient with Waldenström's macroglobulinemia. The IgG-binding site was localized to the F(ab′)2µ fragment of the IgM molecule and the activity was shown to be specific for structures present in the Fcγ fragment of the IgG. µ-and κ-chain fractions were isolated from the IgM after reductive cleavage. Recombination of equimolar quantities of these fractions through both non-covalent and disulfide bond formation resulted in significant levels of anti-IgG activity, as measured by the agglutination of IgG-coated tanned erythrocytes and precipitation of heat-aggregated IgG. This activity was detected shortly after recombination and increased to a maximum after 2 or 3 weeks of storage at 2°C. Ultracentrifugal studies demonstrated that the active products were heterogenous and sedimented over the range of approximately 16S to 40S. Neither chain was active when carried through the recombination procedure in the absence of the other. Maximum anti-IgG activity was recovered from mixtures containing equimolar or greater quantities of the κ-chains. Also, only insignificant levels of activity were detected upon substitution of µ- or κ-chains from another Waldenström's protein that did not bind IgG. The results demonstrated that active molecules were regenerated from the separated polypeptide chains of the IgM and indicate that both chains contributed to the formation of the active site.
Quantitation of Mouse Mammary Tumor Virus (MTV) Virions by Radioimmunoassay
Authors: Cardiff Robert D. 
Published: December 2022

Abstract
A quantitative radioimmune assay for the mouse mammary tumor virus (MTV) has been developed. The assay used highly purified MTV virions which were enzymatically externally labeled with 125I. The radioimmune precipitation (RIP) of 125I-MTV with anti-MTV was specifically inhibited with unlabeled MTV. The degree of inhibition of RIP was directly related to the quantity of unlabeled MTV added. The assay reproducibly detected as little as 5 ng of intact virus. The RIP of 125I-MTV with anti-MTV was not inhibited by murine mammary cell extracts, milk, or “C-type” virus particles. Important variables in this system are discussed.
Quantitative Phagocytosis by Neutrophils
Authors: Ward P. A. , Zvaifler N. J. 
Published: December 2022

Abstract
By using the radiolabeled immune complex method for studying phagocytosis by neutrophils, release of the following lysosomal enzymes has been demonstrated: the C5-cleaving enzyme, β glucuronidase, and acid phosphatase. Enzyme release is directly proportional to cell uptake of immune complexes and is suppressed in antigen excess. It has also been shown that human IgM rheumatoid factor, but not IgM lacking in rheumatoid factor activity, inhibits phagocytic uptake of immune complexes and, correspondingly, depresses the release of lysosomal enzymes.
Isolation of Mucin from Human Submaxillary Secretions
Authors: Baig M. Mansoor , Winzler Richard J. , Rennert Owen M. 
Published: December 2022

Abstract
Human submaxillary mucin isolated by precipitation with cetyltrimethylammonium bromide dissolved in 3 M sodium chloride was subjected to gel filtration on Sephadex G-200. This glycoprotein was free of contaminating proteins as determined by gel filtration, disc electrophoresis, and immunologic studies. The molecular weight was between 500,000 and 1,000,000. The amino acid composition was similar to submaxillary mucins from other species; however, the carbohydrate composition of human mucins varied significantly from different individuals. The mucin from secretor, blood group A individuals is completely absorbed by columns of anti-A antibody coupled with Sepharose 4B, indicating that the submaxillary mucin and the blood group substances in saliva are identical.
Systemic Immunity after Local Antigenic Stimulation of the Lymphoid Tissue of the Gastrointestinal Tract
Authors: Rothberg Richard M. , Kraft Sumner C. , Michalek Suzanne M. 
Published: December 2022

Abstract
The distribution of antibody-producing cells (APC) in the lymphoid tissues of rabbits orally immunized to a low concentration of bovine serum albumin (BSA) was compared to that found in intravenously (i.v.) or subcutaneously (s.c.) immunized animals by determining the concentration of direct and indirect plaque-forming cells in the lymphoid tissues. The spleen was the major site of APC in the i.v. immunized animals and APC predominated in the peripheral lymph nodes of the s.c. immunized group. In contrast, a major site of APC in the orally immunized animals was not directly identified. The concentrations of APC in the spleens of the orally immunized animals were similar to those in the s.c. immunized group, and a relative absence of APC was found in the peripheral and mesenteric lymph nodes, appendix, and Peyer's patches from orally immunized animals.
For determining if systemic immunity is acquired in orally immunized animals in the absence of antibody production by systemic lymphoid tissues, rabbits ingesting the antigen for several weeks were given 50 mg BSA i.v. and the concentrations of APC in the systemic lymphoid tissues were determined 3 days later. Plaque-forming cells were not detectable 3 days after an i.v. injection of BSA given to previously nonimmunized animals, although at this time a marked increase in their concentration was detected in the lymphoid tissues of the i.v. challenged-orally immunized animals.
These studies provide additional evidence that after local antigenic stimulation at gastrointestinal mucosal surfaces, the major site of both secretory and circulating antibody production is the gut-associated lymphoid tissues and that the systemic lymphoid tissues acquire the capacity to produce anti-BSA.
Immunoglobulin on the Surface of Human Lymphocytes. The Detection of Kappa Chain V Region Determinants on B Cells and not on T Cells
Authors: Grey Howard M. , Colon Sonia , Solomon Alan , McLaughlin Carla L. 
Published: December 2022

Summary
Anti-Vκ region antisera and anti-Cκ,λ region antiserum were used to investigate the nature of antigen recognition units of T cells. The results did not support the hypothesis that T cells contain relatively large amounts of V regions with undetectable amounts of C regions which are buried in the membrane but indicated that with specific anti-κI and anti-κIII antisera the detectable V region determinants were confined to the B cell population.
Thymus Dependence of Lymphocyte Trapping
Authors: Zatz Marion M. , Gershon Richard K. 
Published: December 2022

Abstract
Two models were employed to demonstrate the role of the thymus and T cells in antigen-induced lymphocyte trapping: 1) A graft-vs-host response (GVHR) of parental thymocytes to the antigens of lethally irradiated F1 mice; 2) Challenge of T cell-deprived and reconstituted mice with sheep erythrocytes or keyhole limpet hemocyanin. In both experimental situations T cell-dependent augmented localization of 51Cr-labeled cells was demonstrable in the lymphoid tissues. Adult thymectomy and/or irradiation without T cell supplementation diminished, but did not always abrogate, the trapping response. In the GVHR, trapping preceded the peak DNA synthetic response of the parental thymocytes, and correlated with the dose of injected cells.