Journal of immunogenetics最新文献

{"title":"Inactivation of HL-A antigens in vitro by action of antibiotics.","authors":"A Májský,&nbsp;V Chudomel","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The effect of antibiotics on lymphocyte HL-A antigens in vitro is of variable character. All antibiotics under examination suppressed the absorption capacity of HL-A antigens after 2 hr of lymphocyte treatment at 37 degrees C. Ceporin and Kanamytrex inhibited even the cytotoxic reactivity of Hl-A antigens after 15-30 min of lymphocyte treatment. Chloramphenicol, aureomycin, streptomycin and oleandomycin, on the contrary, increased the specific cytotoxic reactivity of HL-A antigens after 15-30 min, after 1 hr they were ineffective for HL-A antigens, and after two or more hours they produced polyreactivity. Penicillin and erythromycin produced polyreactivity after only 15-30 min. The results show that for the follow-up of the drug effect on HL-A antigens the absorption test rather than the cytotoxicity test is of importance. The suppressed absorption capacity of HL-A antigens caused by the action of antibiotics proves their inactivation effect on the lymphocytes. The possibility of an analogous effect of antibiotics on lymphocyte HL-A antigens, even after administration to patients, is discussed.</p>","PeriodicalId":76008,"journal":{"name":"Journal of immunogenetics","volume":"3 1","pages":"29-33"},"PeriodicalIF":0.0,"publicationDate":"1976-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12114909","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Immunochemical observations on the human blood group P system.","authors":"W M Watkins,&nbsp;W T Morgan","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Haemagglutination inhibition experiments were carried out with anti-P1, anti-Pk and anti-P sera in an attempt to increase understanding of the chemical, genetical and serological relationships within the P system. The test-substances comprised a glycoprotein with human blood group P1 and Pk activity isolated from sheep hydatid cyst fluid, fragments isolated from the partial acid hydrolysis products of the P1Pk active glycoprotein, glycolipids, monosaccharides and di- and oligo-saccharides of known structure. The trisaccharide alphaGal(1 leads to 4)betaGal(1 leads to 4)GlcNAc isolated from the glycoprotein hydrolysis products, and earlier established as the P1 determinant (Cory et al., 1974), was the only low molecular weight compound that gave strong inhibition with human, rabbit and goat anti-P1 sera. A disaccharide alphaGal(1 leads to 4)Gal, also isolated from the glycoprotein hydrolysis products, failed to react with anti-P1 reagents but inhibited human anti-Pk sera as strongly as the trisaccharide. The glycolipid alphaGal(1 leads to 4)betaGal(1 leads to 4)Glc-Cer (Ceramide trihexoside) and other oligosaccharides containing alphaGal(1 leads to 4)Gal at the non-reducing terminal were also strong inhibitors of anti-Pk sera. Oligosaccharides with terminal alpha-galactosyl residues joined in other positional linkages gave definite, although less strong, inhibition. The inhibition results suggest a close structural relationship between the P1 and Pk determinants and indicate that the specificity of anti-Pk sera is less closely delineated than that of anti-P1. Human anti-P sera differed markedly from anti-P1 and anti-Pk and were not inhibited by any of the compounds containing alpha-galactosyl residues. The glycolipid betaGalNAc(1 leads to 3)alphaGal(1 leads to 4)betaGal(1 leads to 4)Glc-Cer (globoside) strongly inhibited the anti-P sera. The inhibition of anti-Pk and anti-P sera by ceramide trihexoside and globoside, respectively, confirms the observations of Naiki & Marcus (1974) and supports their conclusions that Pk is the precursor of P. The genetic relationship of the P1 antigen to P and Pk is not clear but biosynthetic pathways are discussed that might explain the absence of P1, Pk and P antigens in individuals of the p phenotype.</p>","PeriodicalId":76008,"journal":{"name":"Journal of immunogenetics","volume":"3 1","pages":"15-27"},"PeriodicalIF":0.0,"publicationDate":"1976-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12114908","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Common origin and evolution of variable and constant regions of immunoglobulins.","authors":"C Wuilmart,&nbsp;J Urbain","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Sequence data show that the immunoglobulins evolved from two sets of paralogous genes: a gene set coding for the V regions and another for the different C regions. A comparison of sequences from these two gene sets shows homology between the V and C sets of genes: this homology is only significant when VH is compared with Cmu1, Cmu2 and Cgamma1. There is a close agreement between our data drawn from sequence comparisons and the data of Poljak et al. (1974) drawn from crystallographic data. This finding is in agreement with the results of the phylogenetic trees of the C and V gene sets: they suggest that the VH subgroups and the first constant domain of the heavy chains are the most ancient. Moreover homology between the red blood cell glycophorin and Cmu2 suggests that immunoglobulins could have a common origin with some membrane proteins.</p>","PeriodicalId":76008,"journal":{"name":"Journal of immunogenetics","volume":"3 1","pages":"1-14"},"PeriodicalIF":0.0,"publicationDate":"1976-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12114907","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}