bluuebunny/crossref_metadata_2025_split huggingface dataset:
Synthesis of C4 by C4 Deficient NIH-Albany Strain Guinea Pig Radiation Chimeras: Restoration of the Classical Pathway of Complement
Authors: Rudofsky U. H. , Webster R. O. , Pickering R. J. 
Published: December 2022

Abstract
We have detected significant hemolytic C4 activity after transplant of normal guinea pig bone marrow into lethally irradiated guinea pigs genetically deficient in C4. Each of five C4-deficient guinea pigs received 640 rads total body irradiation. They were immediately injected intracardially with 93 to 200 × 106 allogeneic nucleated marrow cells from Albany strain normal guinea pigs. The recipients were followed by sequential white cell counts and titrations of total complement, C1, C4, and C2. C4 activity, initially undetectable, was present as early as 24 days after transplantation and reached maximum levels by 45 to 60 days. C4 protein was also identified by using monospecific anti-guinea pig C4 serum. Amounts of C4 were sufficient to restore classical pathway function. C1 activity, initially 2 S.D. below normal, rose dramatically to normal or greater than normal levels. C2 activity also increased. These data demonstrate that allogeneic donor stem cells protected the lethally irradiated C4-deficient recipients and these allogeneic radiation chimeras subsequently synthesize circulating functional C4.
Complex Formation of Properdin Factor B with C3b, an Essential Step in the Generation of the C3b Dependent C3 Cleaving Enzyme of the Properdin System
Authors: Vogt W. , Dames W. , Schmidt G. , Dieminger L. 
Published: December 2022

Abstract
Earlier studies demonstrated that in the presence of Mg++ human factor B interacts with C3b as obtained by trypsin treatment of human C3, and only subsequent to this interaction can be cleaved and activated by Factor D̄. Mg++-dependent binding of highly purified B to C3b was demonstrated by the use of agarose to which trypsin-activated C3̄ had been fixed (Vogt et al., Z. Immunitaet forsch 149:440, 1975). Highly purified human C3b has now been prepared by treating partially purified C3hu with an insolubilized CVFB̄ complex, and fractionating the product on DEAE-cellulose and OH-apatite. The C3b preparation gave a single precipitation line in immunoelectrophoresis with anti-whole human serum, developed fusing precipitation bands with anti-C3c and anti-C3d sera in double immunodiffusion and did not react with antiserum against the B antigen of human C3. C3b and Mg++ were essential for cleavage of B by D̄ and for generation of C3-cleaving activity.
Characterization of Two Species of Fc Fragments Obtained from Rat IgG2a by Prolonged Papain Digestion
Authors: Arend William P. , Hermodson Mark A. , Teller David C. 
Published: December 2022

Abstract
Prolonged papain digestion of rat IgG2a produced two molecular species of Fc fragments, termed Fc(I) and Fc(II). Studies by gel filtration chromatography and polyacrylamide gel electrophoresis in SDS/urea indicated that the two subunit polypeptide chains in each Fc preparation were associated by non-covalent bonds only. By analytical ultracentrifugation Fc(I) was found to have a m.w. of 47,100 and a sedimentation coefficient of 4.08S. Fc(II) had a m.w. of 39,800 and a sedimentation coefficient of 3.83S. The m.w. for the subunit chains of Fc(I) and Fc(II) were 25,300 and 20,300, respectively, as determined by analytical ultracentrifugation under dissociating conditions. Calculation of the frictional coefficient ratios indicated that both Fc fragments possessed compact globular structures.
The difference in size between these two Fc fragments probably was due to a loss of some carboxy-terminal residues in Fc(II). Both Fc fragments possessed nearly identical amino-terminal amino acid sequences. Papain cleavage occurred primarily between residues 233/234 and 234/235. The carbohydrate compositions of the two species of Fc fragments were similar.
It was concluded that under acid and reducing conditions papain cleavage of rat IgG2a occurred to the carboxy-terminal side of the hinge region. Prolonged papain digestion led to secondary attack in the carboxy-terminal end of the Cγ3 domain at an unidentified site, or sites, producing a stable second species of Fc fragments.
Catabolism and Biologic Properties of Two Species of Rat IgG2a Fc Fragments
Authors: Arend William P. , Webster Douglas E. 
Published: December 2022

Abstract
Prolonged papain digestion of rat IgG2a has recently been shown to yield two species of Fc fragments, termed Fc(I) and Fc(II). The results of structural studies indicated that Fc(II) fragment was 15 to 20% smaller than Fc(I), probably secondary to loss of a carboxy-terminal peptide.
The effects of these structural alterations on the catabolism and biologic properties of the Fc fragments were determined. The results of catabolic experiments indicated that after injection into normal rats Fc(I) fragments were retained in the circulation and slowly catabolized whereas Fc(II) fragments rapidly underwent filtration in the kidneys. In nephrectomized rats, however, both Fc(I) and Fc(II) fragments possessed identical slow rates of catabolism, as determined by serum disappearance and whole body catabolic experiments. Fragment pFc′, corresponding to Cγ3 domain, was different from either of the Fc fragments in exhibiting rapid rates of catabolism in both normal and nephrectomized rats. Fc(I) was more active in complement fixation and in adherence to the Fc receptor on monocytes in comparison with Fc(II).
These results support the conclusion that catabolism of Fc and maintenance in circulation are separate processes influenced by different structures in the Fc fragment. The catabolism of Fc is controlled by structures in the Cγ2 domain. This process probably is not related either to complement fixation or to adherence to the Fc receptor on monocytes. Some correlations between the structure and biologic properties of these Fc fragments are discussed.
A New Histogenetic Method for Minor Histocompatibility Antigen Typing
Authors: Hauptfeld Věra , Klein Jan 
Published: December 2022

Abstract
A new method for typing minor H antigens is described. The method is based on the observation that effector T cells, sensitized in vivo to minor H antigens and then rechallenged in vitro, will lyse labeled target cells in the CML assay, provided that the target, the sensitizing, and the responding cells share the same allele at H-2K or H-2D loci. In this method, two congenic lines differing at a minor H locus are cross-immunized (by skin grafting, injection of lymphoid cells, or, preferably, by a combination of both treatments), rechallenged in vitro, and tested against a panel of strains carrying the same H-2 haplotype as the two lines. Target cells of the panel carrying the same minor H antigens as the strain against which the effector cells were sensitized are lysed; target cells not carrying these antigens are unaffected. The feasibility of the method was demonstrated by testing for H-3 antigens of a panel of H-2b-bearing strains. The new method is faster and more economical than the classicial F1 method which has been used until recently.
Bullous Pemphigoid Antigen: Isolation from Normal Human Skin
Authors: Diaz Luis A. , Calvanico Nickolas J. , Tomasi Thomas B. , Jordon Robert E. 
Published: December 2022

Abstract
A protein moiety from epidermal PBS-soluble products was isolated by gel filtration (Bio-Gel A-1.5m) and ion exchange chromatography (DEAE-cellulose). This protein (A-1-Epid) was not retarded by DEAE-cellulose in Tris-HCl buffer, 15mM, pH 8.1. By IEP against an antiserum to epidermal antigens, it showed a single cathodal arc. On disc electrophoresis, at low pH (4.3) a single band was apparent. On SDS gels this protein demonstrated two bands, one with a molecular weight of 20,000, and the second with a molecular weight of 9,200. This purified antigen was able to block the staining of the basement membrane zone produced by bullous pemphigoid antibodies on monkey esophagus and normal human skin with the use of indirect immunofluorescence. This study also demonstrates that bullous pemphigoid antigen (A-1-Epid) and a second epidermal protein (A-2-Epid) are present in the PBS-soluble products of human esophageal mucosa, saliva, and urine. These antigens appear to be unrelated with the blood group substances or secretor status of the donors.
Cyclophosphamide-Induced Specific Suppression of the Protective Immune Response to Rodent Malaria
Authors: Wells Robert A. , Diggs Carter L. , Phillips S. Michael 
Published: December 2022

Abstract
Nonspecific and specific chemosuppression of the immune response to Plasmodium berghei protective antigens were investigated. Specific immunosuppression was defined operationally as the selective suppression of the protective response to the parasite in mice injected with a combination of γ-irradiated infected mouse erythrocytes (γPb) and cyclophosphamide (CY) with continued responsiveness to sheep erythrocytes (SRBC). After initial treatment (γPb + CY), mice were injected with γPb in potentially immunogenic doses. These and appropriate control animals were later challenged with nonirradiated infected mouse erythrocytes. The influence of the initial treatment regimens on the protective response was evaluated by parasitemia, and mortality was observed after challenge. Specificity of suppression was measured by evaluating the ability of mice to produce antibody to SRBC.
Both specific and nonspecific suppression of the protective response to malaria were noted. Initial treatment with drug alone resulted in increased parasitemia and mortality and suppression of the SRBC antibody synthesis in drug-pretreated immunized mice as compared with immunized mice not pretreated with the drug. On the other hand, suppression of the response to the parasite, but not to SRBC, in animals pretreated with γPb + CY was clearly greater than that induced by drug alone. Thus, animals treated with malarial antigen and cyclophosphamide develop a measurable specific immunosuppression. These studies indicate that immunity to malaria is influenced by both cyclophosphamide alone (general immunosuppression) and cyclophosphamide in combination with antigen (specific immunosuppression) in a manner analogous to other immune responses.
Antibody-Mediated Suppression of Tumor Growth
Authors: Johnson Robert J. , Pasternack Gary R. , Shin Hyun S. 
Published: December 2022

Abstract
The effectors that cooperate with IgG1 in causing tumor suppression were identified as exudate macrophages and blood platelets in animals syngeneic and allogeneic to the tumor. Lymphocytes were not active in suppressing tumor growth in the presence of IgG1 antibody, although they were active with whole antiserum.
Studies of the Mechanism of the Human Platelet Release Reaction Induced by Immunologic Stimuli
Authors: Pfueller Sharron L. , Weber Susanne , Lüscher Ernst F. 
Published: December 2022

Abstract
Aggregated IgG coupled covalently with bis-diazobenzidine (BDB-IgG) and labeled with 3H-diazobenzene (3H-BDB-IgG) has been used to study the binding of soluble IgG aggregates to human platelets in relationship to the release of the contents of intracellular granules (e.g., serotonin). In washed cell suspensions a minimum of 0.14 to 0.2 µg 3H-BDB-IgG per 5 × 108 platelets (40 to 70 aggregates per cell) was required for the triggering of the release reaction and cell aggregation. Binding was independent of divalent cations. The Arrhenius plot gave a straight line between 0 to 37°C and a Q10 of 1.6. Neither inhibitors of the release reaction nor energy metabolism, nor formaldehyde fixation of the platelets affected binding. Bound 3H-BDB-IgG was not significantly eluted by IgG, bovine albumin (BSA), buffer, or plasma.
Binding to washed platelets was more strongly inhibited by human IgG than by F(ab′)2, bovine IgG, human albumin (HSA), or BSA. Plasma was an even more effective inhibitor of both binding and release. Plasma deficient in IgG or depleted of complement retained its inhibitory capacity. In the presence of plasma, at physiologic ratios of plasma and platelets, no release of serotonin was observed. Binding, although inhibited in rate, nevertheless occurred. It was enhanced by divalent cation chelation and had a Q10 of 2.5.
The release reaction of washed platelets to which 3H-BDB-IgG had been bound in the presence of HSA or BSA was also inhibited by the subsequent addition of plasma or plasma proteins (human IgG being more effective than bovine IgG, F(ab′)2, HSA, or BSA). 3H-BDB-IgG bound in the presence of either plasma or human IgG did not induce release when the platelets were subsequently suspended in media lacking these proteins. Thus, it appears that the platelet Fc receptor binds 3H-BDB-IgG by a process which is effectively inhibited by plasma, or by free IgG with an intact Fc, and to some extent by high concentrations of other proteins. The effects of bound IgG aggregates are dependent on the other proteins present both during binding and subsequently added. The mechanism of such receptor modulation and its implications in vivo are discussed.
Complement Activation by Measles Virus Cytotoxic Antibodies: Alternative Pathway C Activation by Hemagglutination-Inhibition Antibodies but Classical Activation by Hemolysin Antibodies
Authors: Ehrnst Anneka C. 
Published: December 2022

Abstract
Antibodies against measles virus hemagglutinating (HA) particles and hemolysin were shown to activate C differently. HA antibodies of rabbit or human origin activated C via the alternative pathway in cytotoxicity against chronically measles-infected cells. This cytotoxicity was expressed in C-4 deficient guinea-pig C or in rabbit C in the presence of 3 mM EGTA (ethylene-glycol-tetraacetic-acid) but not in 3 mM EDTA (ethylene-diamine-tetraacetic-acid). In contrast, human hemolysin antibodies activated C only via the classical way.
F (ab′)2 fragments from rabbit or human anti-HA IgG antibodies were as efficient in C activation via the alternative pathway as intact IgG antibodies with a corresponding hemagglutination-inhibition titer.
Antigen Recognition: The Specificity of an Isolated T Lymphocyte Population
Authors: Stashenko Philip P. , Schlossman Stuart F. 
Published: December 2022

Abstract
Guinea pig lymph node lymphocytes were separated into T and B cell fractions on immunoabsorbent columns. Separated cells were functionally distinct: T cells proliferated in response to ConA, PHA, soluble and alloantigen, whereas anti-Ig reagents only stimulated B cells. The in vitro proliferative response of guinea pig lymph node T lymphocytes was then shown to be highly discriminating when elicited by a series of structurally similar synthetic DNP-oligolysine antigens. Proliferation was always most extensive in response to the homologous, immunizing antigen, and less intense to cross-reacting DNP-oligolysines. Specificity of proliferation was maintained in the absence of both B lymphocytes and antibody secreting cells, suggesting that T cell recognition is not “acquired” from B cells or secreted antibody, but is a property inherent to the T cell.
Antigen-Specific T Cell Factors: A Fine Analysis of Specificity
Authors: Isac Ronit , Mozes Edna 
Published: December 2022

Abstract
The specificity of T cell factors produced in presence of synthetic polypeptide antigens was studied. Factors prepared with either one of the three antigens: poly(Tyr,Glu)-poly(DLAla)--poly(Lys), (T,G)-A--L, poly(Phe,Glu)-poly(DLAla)--poly(Lys), (Phe,G)-A--L, and poly(His,Glu)-poly(DLAla)--poly(Lys), (H,G)-A--L, successfully cooperated with B cells for antibody production to the homologous as well as to the other two immunogens. Furthermore, the activity of a (T,G)-A--L-specific factor was removed after passage through immunoadsorbents built of Sepharose coupled to: (T,G)-A--L, (Phe,G)-A--L and poly(Glu)-poly(DLAla)--poly(Lys), (G)-A--L, but not to poly(DLAla)--poly(LLys), A--L. No cross-reactivity was observed between (T,G)-A--L and poly(Tyr,Glu)-poly(Pro)--poly(Lys), (T,G)-Pro--L, at the level of T cell factors, as shown using the above approaches. These results lead to the conclusion that specificity of T cell factors, although not identical, is similar to that of antibodies.
Schistosomiasis in the Congenitally Athymic (Nude) Mouse
Authors: Phillips S. Michael , DiConza Joseph J. , Gold Jerome A. , Reid Willis A. 
Published: December 2022

Abstract
Athymic nude mice (Nu/Nu), heterozygous littermates (Nu/+), and thymus reconstituted homozygous animals (Nu/Nu TxR) were exposed to Schistosoma mansoni cercariae. A marked impairment in the development of peripheral blood eosinophilia and hepatic granuloma was observed in the Nu/Nu animal. In addition, host morbidity judged by organ weight, portal pressures and reticuloendothelial activity were less in the Nu/Nu animal. Thymus-reconstituted animals demonstrated eosinophilia, increased granuloma size, and morbidity equivalent to that shown by the Nu/+ heterozygous littermates. These studies indicate that the eosinophilia, granulomatous hypersensitivity, and ultimate host morbidity, associated with murine schistosomiasis, is dependent on thymic dependent lymphocyte function.
Enhancement by Irradiated T Cells of Human Plasma Cell Production: Dissection of Helper and Suppressor Functions in Vitro
Authors: Siegal Frederick P. , Siegal Marta 
Published: December 2022

Abstract
The addition of irradiated T-enriched lymphocytes to B cell-enriched fractions of human peripheral blood or to unseparated mononuclear cells stimulated the differentiation of plasmacytoid cells in culture with pokeweek mitogen beyond the synergy obtained by the addition of unirradiated T cells. This stimulation was observed in both the proportion and absolute number of plasmacytoid cells recovered from the cultures, and in the amount of IgM detected in culture supernatants by a hemagglutination inhibition assay. Irradiation-induced enhancement was observed with normal and hypogammaglobulinemic T cells, but not with monoclonal T cells from two patients. Inactivation of T cells by heating or by repeated freezing and thawing did not produce the same effects as did irradiation. These data suggest that cell-mediated suppressor function in man is selectively radiosensitive, while helper activity is not. Irradiation may be a useful method for the functional isolation of helper cells and for the manipulation of the balance between suppressor and helper cell activities.
Complement-Induced Histamine Release from Human Basophils
Authors: Hook William A. , Siraganian Reuben P. 
Published: December 2022

Abstract
Human serum activated with zymosan generates a factor (C5a) that releases histamine from autologous basophils. Previously we have presented evidence that this mechanism for C5a-induced release differs from IgE-mediated reactions. The effect of several pharmacologic agents known to alter IgE-mediated release was studied to determine whether they have a similar action on serum-induced release. Deuterium oxide (D2O), which enhances allergic release, inhibited in a concentration-dependent fashion the serum-induced reaction at incubation temperatures of 25 and 32°C. The colchicine-induced inhibition was not reversed by D2O. Cytochalasin B, which gives a variable enhancement of IgE-mediated release, had a marked enhancing effect on the serum-induced reaction in all subjects tested. The following agents known to inhibit the IgE-mediated reaction also inhibited serum-induced release at 25°C: colchicine, dibutyryl cyclic AMP, aminophylline, isoproterenol, cholera toxin, chlorphenesin, diethylcarbamazine, and 2-deoxy-D-glucose. These results suggest that the serum-induced release is modulated by intracellular cyclic AMP, requires energy, and is enhanced by the disruption of microfilaments. The lack of an effect by D2O would suggest that microtubular stabilization is not required. The data can be interpreted to indicate that IgE- and C5a-mediated reactions diverge at a late stage in the histamine release pathway.
Characterization of DNA Used to Assay Sera for Anti-DNA Antibodies; Determination of the Specificities of Anti-DNA Antibodies in SLE and Non-SLE Rheumatic Disease States
Authors: Locker Joseph D. , Medof M. Edward , Bennett Robert M. , Sukhupunyaraksa Surintra 
Published: December 2022

Abstract
Commercial 14C-labeled KB cell DNA, widely used to assay sera for anti-DNA antibodies, was chromatographed on benzoylated-naphthoylated-DEAE-cellulose (BNDC) and on hydroxyapatite (HAP). On BNDC, only 25% of the 14C label eluted with 1 M NaCl (KB fraction I) characteristic of ds-DNA. Fifty-five percent of the label eluted with 50% formamide-1 M NaCl (KB fraction II) characteristic of ss or denatured DNA. On HAP, however, none of the 14C label eluted with 0.2 M phosphate buffer as anticipated for ss-DNA, but, rather, all of the 14C label eluted with 0.4 M phosphate, characteristic of ds-DNA. After pretreatment with S1 endonuclease of Aspergillus oryzae, which selectively digests ss regions, however, 42% of the 14C label was lost from the 0.4 M phosphate peak. These results indicated that more than half of this 14C-KB-cell DNA preparation was ds-DNA with ss regions which was undetectable by HAP chromatography. 3H-ds-DNA and circular 3H-ss-DNA prepared from T7 and øX174 bacteriophage, respectively, were found to be chromatographically pure on both BNDC and HAP.
None of 10 non-SLE sera (rheumatoid arthritis 3, mixed connective tissue disease 4, scleroderma 1, ulcerative colitis 1, and pulmonary fibrosis with chronic active hepatitis 1), previously believed to contain anti-ds-DNA antibodies on the basis of KB cell DNA testing had detectable antibodies against KB fraction I or T7 DNA: all of 10 KB cell DNA positive SLE sera had antibodies against both. Additionally, none of the 10 non-SLE sera had antibodies against KB cell DNA when retested with DNA that had been pretreated with S1 endonuclease. Seven of these 10, however, as well as all 10 SLE sera, had antibodies against øX174 DNA, KB fraction II DNA and alkali-denatured T7 DNA.
The data support the conclusions that 1) false positive tests for anti-ds-DNA antibodies can result from contamination of ds-DNA with ds-DNA having ss regions, and 2) non-SLE sera do not contain antibodies specific for ds-DNA at levels comparable to those found in SLE sera but rather contain high levels of antibodies reacting with ss regions or mixed DNA.
On the Biochemical Racial-Index of the Ainu, Gilyak and Orokko in Karafuto (Saghalien)
Authors: Kishi Takayoshi 
Published: December 2022

Abstract
It is well known that we can classify all human blood into four different groups by isohemagglutination (Landsteiner (1), Jansky (2), Moss (3), v. Dungern (4) and Hirschfeld); namely,
Group I or O. The serum agglutinates the cells of groups II, III, and IV. The cells are agglutinated by no serum.
Group II or A. The serum agglutinates the cells of groups III and IV. The cells are agglutinated by the serum of groups I and III.
Group III or B. The serum agglutinates the cells of groups II and IV. The cells are agglutinated by the serum of groups I and II.
Group IV or AB. The serum agglutinates no cells. The cells are agglutinated by the serums of groups I, II, and III.
To explain this phenomenon, we must assume the existence of two agglutinable substances, A and B in the corpuscles and two agglutinins, α and β in the serum, distributed in the groups as follows.