bluuebunny/crossref_metadata_2025_split huggingface dataset:
Human and Rat γ E: Serologic Evidence of Homology
Authors: Kanyerezj B. , Jaton J.-C. , Bloch K. J. 
Published: December 2022

Abstract
The homocytotropic (reaginic) antibodies of several mammalian species resemble one another in their occurrence in trace amounts in serum following immunization, in their heat and sulfhydryl lability, and in their firm binding to target (mast) cells (1). Based on physicochemical characteristics, these homocytotropic antibodies have been identified as γE immunoglobulins in man, monkey, rabbit and rat (2–5). Antigenic relationships among the γE immunoglobulins of these species have been noted (3, 4, 6); the present report concerns the antigenic relationship between human γE (represented by myeloma protein PS (7)) and rat γE (represented by rat anti-Nippostrongylus brasiliensis homocytotropic antibodies (8)).
Human myeloma proteins of the γG, γA, γD and γE class and a Waldenström γM protein were isolated by starch block electrophoresis, anion exchange chromatography and gel filtration according to conventional methods.
Immunologic and Immunochemical Studies on the Gar, Lepisosteus Platyrhincus
Authors: Bradshaw Claire M. , Clem L. William , Sigel M. Michael 
Published: December 2022

Abstract
Purified gar 14S immunoglobulin, obtained by DEAE-cellulose chromatography followed by Sephadex G-200 gel filtration, was found to have a molecular weight of ∼650,000 and a relatively high hexose content, and to be composed of disulfide-linked H (m.w. ∼70,000) and L (m.w. ∼22,000) polypeptide chains present in equimolar amounts. Based upon these data it is proposed that this 14S protein is a tetrameric form of IgM. Immunoelectrophoretic analysis of fractions from Sephadex G-200 with rabbit anti-gar H- and L-chain antisera indicated that this was the only class of immunoglobulin present in gar serum.
Detection of Cell-Absorbed Protein Antigen by an Equilibrium Diffusion Method
Authors: Tai Chiaki , McGuigan James E. 
Published: December 2022

Abstract
Diffusion dialysis experiments were conducted using cellulose polyacetate membranes permeable to protein antigen (125I-BGG) but not to cells and microscopically visible cellular components. Under the conditions of these experiments the binding of 125I-BGG by peritoneal exudate cells from non-immunized guinea pigs could not be detected. It was possible to detect and semiquantify binding of 125I-BGG by nonimmunized peritoneal exudate cells which had been pretreated with antiserum containing cytophilic antibodies to BGG. This method, which detects the binding of antigen macromolecules, may be applicable to the study of receptor sites on the surfaces of sensitized lymphocytes postulated to be important in cell-mediated hypersensitivity.
Lymph Node Cells Carrying Receptor Sites Detected by Diffusion Dialysis Techniques
Authors: Tai Chiaki , McGuigan James E. 
Published: December 2022

Abstract
Hartley strain guinea pigs were immunized with bovine γ globulin (BGG) using various techniques in order to produce humoral antibodies, delayed hypersensitivity or both humoral antibodies and hypersensitivity to BGG. A diffusion dialysis technique was utilized to demonstrate cell binding of antigen (125I-BGG). Cells contained in regional lymph node preparations from guinea pigs with delayed hypersensitivity to BGG demonstrated high degrees of cell binding of 125I-BGG. Cytophilic antibodies to BGG were also produced in some guinea pigs. The results of these studies fail to demonstrate a relationship between cell binding of antigen associated with the development of delayed hypersensitivity and the presence of cytophilic antibodies.
Antibody-Agarose Immunoadsorbents: Complete Removal of Classes of Immunoglobulins from Serum
Authors: Mannik Mart , Stage David E. 
Published: December 2022

Summary
Purified antibodies to human γG, γA and γM and to κ and λ chains were prepared with antigen-agarose immunoadsorbents. The purified antibodies were used to prepare antibody-agarose adsorbents. These in turn permitted selective and complete removal of individual classes of immunoglobulins from sera. Sequential use of appropriate immunoadsorbents allowed the complete removal of all immunoglobulins from sera.
Secretion of Monospecific Anti-Hapten IgG Antibodies by Rabbit Immunocytes
Authors: Hanna Edgar E. , Merchant Bruce 
Published: December 2022

Abstract
A direct search was made for antibody-forming cells that simultaneously secrete antibodies to two related but non-cross-reacting hapten determinants. This was accomplished by combining the hapten-specific hemolytic plaque technique with the replica immune plaque procedure. Rabbits were immunized intravenously with a particulate immunogen consisting of pigeon erythrocyte membranes coupled with both p-arsanilate and o-sulfanilate determinants. Replica immune hapten-specific plaque assays were performed after immunization intervals of 10 days, 4 months and 6 months. These replica assays showed two separate and distinct populations (anti-p-arsanilate and anti-o-sulfanilate) of IgG-secreting immunocytes. No more than 2% of the 6 × 103 immunocytes screened were potential double secretors, and the average number for all assays was 1.4%. It was possible to artificially produce a similar small percentage (2.5%) of “double” plaques by intentionally mixing two independent monospecific plaque-forming cell suspensions. The study indicates that at any one time the vast majority of IgG-secreting rabbit splenic immunocytes are specialized for the production of antibodies that react with only one of two noncross-reacting hapten determinants.
Role of Macrophages and Antibody in Resistance of Mice against Yellow Fever Virus
Authors: Zisman B. , Wheelock E. F. , Allison A. C. 
Published: December 2022

Abstract
Adult mice were treated with silica and antilymphocytic serum before intravenous inoculation of 17D yellow fever virus. Ingestion of silica particles impaired liver macrophage function and allowed early invasion of virus into the brain. Antilymphocytic serum had no potentiating effect after i.v. inoculation of virus. Passive transfer of antibodies protected silica pre-treated mice against development of a fatal infection. These results are discussed in relation to the role of macrophages and cell-mediated and humoral immunity in protection against blood-borne virus infections.
Immunoelectrophoretic Studies of the California Encephalitis Virus Group
Authors: Wellings F. M. , Sather G. E. , Hammon W. McD. 
Published: December 2022

Abstract
Immunoelectrophoretic studies of the California encephalitis group (CEV) of arboviruses were carried out. Both single and multiple injection rabbit antisera prepared against the various antigens were used in several agar-buffer-pH systems. Multiple shared antigens were demonstrable among BFS-283 (CE) and all other members of the group except Keystone (KEY) and trivittatus (TVT), thus showing a close antigenic relationship among the majority of members. However, only a minor common antigen was shared between CE and the latter two, indicating a distant antigenic relationship. Guaroa, a member of the Bunyamwera (BUN) group shown by the more conventional neutralization and hemagglutination tests to be related to the CEV group, was found to show a common minor antigen with all members of the CEV group except TVT. At least two common antigens were shared with the latter. Based on this present work and immunodiffusion studies previously reported, it is suggested that the CEV group be considered as a separate group with at least three types. These would be represented by prototypes CE, TVT and KEY. More exhaustive antigenic studies may eventually define additional types and further elucidate the extent of relatedness among members of the CEV and BUN groups.
Experimental Allergic Encephalomyelitis: Species Variability of the Encephalitogenic Determinant
Authors: Swanborg Robert H. , Amesse Lawrence S. 
Published: December 2022

Summary
Modifcation of the single tryptophan residue of the basic protein (BP) isolated from bovine brain results in the loss of encephalitogenic activity in guinea pigs. In contrast, when these same modified BP preparations are tested in Lewis rats they still cause experimental allergic encephalomyelitis (EAE). These findings suggest that different encephalitogenic determinants are responsible for EAE in these species.
The Thymus in the Chicken and its Anatomical Relationship to the Thyroid
Authors: Panigraphi D. , Waxler G. L. , Mallman V. H. 
Published: December 2022

Abstract
The surgical removal of either the bursa of Fabricius or the avian thymus has been used to demonstrate their roles in the immunologic maturation necessary for antibody production (1) or delayed sensitivity (2–6), respectively. The bursa is a discrete organ, readily removed. The thymus of the chicken is composed of several lobes which lie above the jugular vein on either side and occupy almost the entire length of the neck. The most posterior lobe is closely adjacent to the thyroid. The number of thymic lobes on each side has been reported to be five (7), seven (8, 9) or to vary from six to eight (10).
We report herein that complete thymectomy of 1-day-old chickens is essentially a surgical impossibility due to the relative positions of the thyroid and posterior lobes of the thymus.
Thirty White Leghorn chickens, 10 each at 1 day, 5 weeks and 10 weeks of age, respectively, were killed and the numbers of thymic lobes on side has been reported to be five (7), seven (8,9) or to vary from six to eight (10).
Alteration in Complement Component Utilization Following the Interaction of C1̄hu with a Kallikrein Fragment
Authors: Gigli I. , Kaplan A. , Austen K. F. 
Published: December 2022

Abstract
A mixture of human IgG, kallikrein and plasma thromboplastin antecedent (PTA) prepared by passage of serum over DEAE-cellulose equilibrated with 0.01 m phosphate buffer, pH 8, was found to enhance the hemolytic activity of activated human first component of complement (C1̄hu). Fractionation of this mixture on Sephadex G-150 revealed peaks of C1̄hu-enhancing activity at 45% bed volume, the position of kallikrein, and at 80% bed volume. Repeat filtration of the kallikrein fraction on Sephadex G-150 yielded the low molecular weight C1̄hu-enhancing factor, suggesting that it was derived from kallikrein. This non-dialyzable fragment lacked kallikrein activity and unlike C1̄s did not split N-α-acetylglycyl-l-lysine methylester (AGLMe), N-acetyl-l-arginine methylester (AAMe), p-tosyl-l-arginine methylester (TAMe), N-acetyl-l-tyrosine methylester (ATMe), the fourth component (C4), or the second component (C2).
Kinetics of C2 activation by C1̄ acting upon EAC42 prepared with limited concentrations of unactivated C2 indicated that C1̄ containing 20 mol/cell produced 0.57 SAC with a tmax of 3.5 min; C1̄ acted upon by the fragment and then diluted sevenfold as compared to the untreated C1̄ produced 1.6 SAC at a tmax of 1.75 min.
C4 Inactivating Factor in C4 Deficient Human Serum
Authors: Torisu M. , Nagaki K. , Inai S. , Sonozaki H. 
Published: December 2022

Abstract
Our inactivating factor for the fourth component of human complement (C4 INF) was partially purified from pseudoglobulin fraction of C4 deficient human serum. Initially C4 INF was thought to specifically inactivate C4; however, after thorough comparison with highly purified active human esterase (C1s), it became clear that both substances share the following activities: 1) Both substances showed SAC4,2 generating activities on EAC4gp cells as well as on EAC4hu cells. 2) Both substances inactivated C2 as well as C4. 3) Both substances hydrolyzed TAMe. 4) Both substances were sensitive to DFP as well as PMSF. 5) SAC4,2 generating activities of both substances were neutralized by anti-C1s. 6) Both substances were not fixed on either EA or EAC4 cells. 7) Both substances showed antigenic identity against anti-C1s by Ouchterlony analysis. 8) Both substances showed the same electrophoretic mobility on acrylamide gel. 9) Both substances altered the electrophoretic mobility of native C4hu in a similar manner.
Isolation and Characterization of a Factor from Human and Guinea Pig Serum That Accelerates the Decay of SAC142
Authors: Opferkuch W. , Loos M. , Borsos T. 
Published: December 2022

Abstract
A factor has been isolated from the pseudoglobulin fraction of human and guinea pig serum which accelerates the decay of SAC142. The decay-accelerating factor (DAF) of guinea pig serum is a heat stable (1 hr, 56°C) α globulin, has a molecular weight of about 300,000 (estimated by gel filtration) and a sedimentation rate of 8.2S; the DAF of human serum has an m.w. of about 170,000. DAF can be adsorbed to E at a rate that is independent of temperature. EA, EAC1, EAC4, EAC14 and EAC142 at the same cell concentration take up the same amount of DAF. The activity of a given amount of DAF is independent of the number of SAC142/EAC142 and is dependent on the number of cells present in the reaction mixture. While DAFhu accelerates the decay of SAC142 made with C2hu, oxyC2hu and C2gp, DAFgp is capable of accelerating the decay of SAC142gp, but not those made with C2 of human origin.
Isolation of the Precursor and the Active Form of the C3 Activator from Human Serum
Authors: Götze O. , Müller-Eberhard H. J. 
Published: December 2022

Abstract
It had previously been shown that a protein isolated from the venom of Naja naja, the cobra factor, is capable of forming a complex with a β globulin present in human serum. This complex is able to cleave C3 in free solution and apparently activates the terminal complement components beginning with C3.
The C3 proactivator (C3PA) which participates in these reactions by forming the enzymatically active complex with cobra factor was isolated from human serum. It was found to be homogeneous on disc- and immunoelectrophoresis.
Cleavage of the C3PA into at least two fragments was observed by treatment of serum with a variety of naturally occurring lipopolysaccharides and polysaccharides such as endotoxin, zymosan, inulin or agar. This reaction was accompanied in all instances by the conversion of C3 to its electrophoretically faster form. The larger of the two C3PA fragments (m.w. approximately 60,000) has γ globulin mobility and is antigenically deficient.
Immunochemical and Biologic Characterization of a New C3 Conversion Product, C3x, Generated in Human Serum in the Absence of C3 Convertase
Authors: Spitzer R. E. , Stitzel A. E. , Pauling V. L. , Davis N. C. , West C. D. 
Published: December 2022

Abstract
C3x, the product of a non-convertase dependent C3 conversion mechanism in normal human serum, appears to be a conformational alteration of the native molecule. It has a molecular weight approximately the same as C3 and its generation is not accompanied by any detectable cleavage of the molecule. C3x bears all three antigens of C3 (A, B, D) but is quantitatively deficient with respect to the native molecule in the amount of antibody consumption to the B antigen. In addition, C3x has a slightly faster mobility in acrylamide gel and agar than does native C3. C3x is extremely stable, resisting cleavage by trypsin up to 1 hr at 37°C, 0.3 M hydroxyl-amine, C, or pH 3.0. Biologically, C3x is unique in that it cannot participate in immune lysis or erythrocyte immune adherence but does interact with C5 and augments erythrophagocytosis. C3x is also markedly chemotactic for human PMN's and causes increased vascular permeability in the guinea pig which is not histamine dependent.
Complement Efficiency in Immune Hemolysis
Authors: Linscott W. D. 
Published: December 2022

Abstract
C1 is fixed very inefficiently by IgG anti-Forssman antibody under physiologic conditions of temperature and ionic strength (µ), and these are the same conditions under which most hemolytic and C fixation reactions are carried out. If washed, IgG-sensitized erythrocytes are incubated with absorbed guinea pig C for 1 hr at 0°C, µ = 0.037, and then diluted with an equal volume of cold buffer at µ = 0.15 and immediately placed at 37°C for 1 hr, a more than 10-fold increase in sensitivity of the assay is obtained (less IgG and less C are needed for hemolysis).
The sensitivity of hemolytic assays for IgM can also be improved, though not so dramatically, by choosing conditions more favorable for C1 fixation. At low antibody concentrations, a severalfold increase in lysis is observed if washed, IgM-sensitized erythrocytes are incubated with absorbed guinea pig C for 1 hr at 37°C, µ = 0.094, instead of µ = 0.15.
Ultrastructural Studies of Clq and of the Interaction Between Membranes and Complement Proteins
Authors: Polley M. J. 
Published: December 2022

Abstract
Ultrastructural studies of human C1q have demonstrated the molecule to exist in two distinct forms. Svehag and Bloth have described the molecule to be composed of six subunits arranged in a disc-like form. Our studies suggest that the disc-like form of the native molecule constitutes a disc-like coil consisting of six subunits which is capable of unfolding to a rod-like structure with an identical number of subunits.
Red cell antibody complement complexes were prepared at various intermediate stages throughout the complement sequence; stroma was prepared from each and examined ultrastructurally. In complexes prepared up to the EAC1,4,2,3 stage in which no lesions were seen, sections of the membranes demonstrated the “tram-line” appearance described for normal red cell membranes by Dourmashkin and Rosse. At the EAC1–5 stage, when lesions first became visible, the membranes seen in section had retained their dense linear appearance; however, they had increased in width from 100 to 250 Å.
Kinetics of Bovine Complement
Authors: Fong Jack S. C. , Muschel Louis H. , Good Robert A. 
Published: December 2022

Abstract
With the use of conglutination assay and different anticomplementary agents, the lytic intermediate formed during interaction of sensitized sheep erythrocytes and diluted bovine serum was shown indirectly to be SHEACBo142. Lysis of this cellular intermediate by guinea pig C3-9 was completed in about 6 min of incubation at 37°C at ionic strengths between 0.075 and 0.125. In contrast to the lability of other corresponding intermediates, SHEACBo142 was extremely stable in low ionic strength buffer (GGBS++) with divalent cations: up to 18 hr at 37°C and 6 days at 2°C. Change of the ionic strength of the buffer to iso-ionicity resulted in gradual decay of the lytic intermediate, whereas presence of EDTA induced a precipitous decay of SHEACBo-142, whose reactivity could be restored with bovine euglobulin or functionally pure human C1. The apparent paradox, that is, that bovine complement was non-hemolytic to sensitized sheep erythrocytes and inhibitory to the lytic activity of guinea pig terminal complement components on SHEACBo142 but hemolytic to sensitized rabbit erythrocytes, further emphasized that in vitvo hemolytic complement assays do not necessarily correlate with in vivo functional activity of complement-dependent or -mediated processes.
Lack of Antibody Activity in Human Myeloma Proteins
Authors: Yoo T. J. , Franklin Edward C. 
Published: December 2022

Abstract
Two hundred and seventy-five myeloma sera were screened with a battery of 20 antigens including 13 haptens, pneumococcal polysaccharides and four bacterial antigens. In no instance was it possible to detect antibody activity by double diffusion in agar or by fluorescence quenching.
Surface Immunoglobulins on Mouse Lymphoid Cells
Authors: Bankhurst Arthur D. , Warner Noel L. 
Published: December 2022

Abstract
Addition of 125I-labeled anti-immunoglobulin protein to cell suspensions from mouse thymus, spleen and thoracic duct lymph (TDL) resulted in labeling of surface immunoglobulins of lymphoid-like cells. Near-optimal conditions for cell labeling were established with varying anti-immunoglobulin concentrations and times of exposure. On the average 20.1% to 36.3% of TDL and spleen cells labeled under such conditions, whereas thymus cells labeled less heavily (0.3% to 3.7%) with identical materials. Normal rabbit sera (NRS) or anti-immunoglobulin absorbed with purified immunoglobulins produced essentially no labeling. The total heavy chain labeling on TDL and spleen cells exceeded light chain labeling (64.6% vs 31.8% and 79.8% vs 33.0%, respectively). This might suggest that labeled cells had multiple surface heavy chain determinants or that the anti-heavy chain antibodies cross-reacted with an unidentified immunoglobulin-like surface antigen. There was increased labeling with TDL suspensions from neonatally thymectomized mice (65% with anti-light chain). This was consistent with the hypothesis that primarily non-thymus-derived cells were labeled by these techniques.
An Efficient Method for Isolation of HL-A Antigens from Hematopoietic Cell Lines
Authors: Miyakawa Y. , Tanigaki N. , Yagi Y. , Pressman D. 
Published: December 2022

Abstract
A simple isolation procedure has been established that gives a high yield of relatively pure HL-A antigens from cells of established hematopoietic cell lines. Particulate HL-A antigens were obtained from cells disrupted by shaking in buffer. These particulates were digested with papain in the presence of cysteine, and the soluble papain fragments that carried antigenic activity were purified by hypotonic dialysis, followed by ion exchange chromatography on DEAE-Sephadex, ultrafiltration, gel filtration and column electrophoresis. Several preparations of soluble HL-A antigens, each carrying one of the representative antigenic activities, HL-A1, HL-A2 or HL-A7, were obtained from three different cell lines. These preparations had a high degree of homogeneity in molecular size (48,000 Daltons) and a narrow range of electrophoretic mobility in the α2 globulin region. In these preparations, the overall recovery of HL-A antigenic activity was 30% to 37% for each isolated specificity, the recovery of OD280 units was 0.08% to 0.14%, the OD280/OD260 ratio was approximately 1.7 and the increase in specific antigenic activity was approximately 300 times that of papain digests.
HL-A Antigens from Hematopoietic Cell Lines: Molecular Size and Electrophoretic Mobility
Authors: Tanigaki N. , Miyakawa Y. , Yagi Y. , Pressman D. 
Published: December 2022

Abstract
HL-A antigens of hematopoietic cells in long-term culture were solubilized by papain digestion, and the molecular size and electrophoretic mobility of the fragments carrying individual HL-A specificities were estimated. HL-A1, HL-A2, HL-A7 and HL-A8 specificities were present on molecular fragments of 48,000 Daltons. An unidentified alloantigenic specificity was present on molecular fragments of 74,000 Daltons. Although all the HL-A active fragments migrated to the α2 globulin region upon electrophoresis, the mobility of the molecular fragments carrying HL-A2 specificity was slightly lower than those of fragments having the other specificities. All papain fragments of HL-A2 specificity from different cell lines were identical in molecular size and electrophoretic mobility. A similar identity also appeared to be present among the papain fragments carrying the other specificities.