{"title":"游离n -乙酰神经氨酸C-5上含硫取代基对Sia-lb1抗原性的增强。","authors":"D Roelcke, A Leo, R Brossmer","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The Sia-lb1 epitope, recognized by anti-Sia-lb1 cold agglutinins, is unique since it is represented by the alpha-N-acetylneuraminic acid (alpha NeuNAc) monosaccharide. Chemical modifications of the chain at C-5 of alpha NeuNAc have shown that the natural 2-carbon and the artificial 3-carbon chains are optimal for anti-Sia-lb1 binding. Sia-lb1 antigenicity of alpha NeuNAc could be tenfold enhanced by replacement of the carbonyl oxygen by sulphur. The structural requirements of the Sia-lb1 epitope for optimal antibody binding were identified.</p>","PeriodicalId":79439,"journal":{"name":"Beitrage zur Infusionstherapie und Transfusionsmedizin = Contributions to infusion therapy and transfusion medicine","volume":"34 ","pages":"215-9"},"PeriodicalIF":0.0000,"publicationDate":"1997-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Enhancement of Sia-lb1 antigenicity by sulphur-containing substituents at C-5 of free N-acetylneuraminic acid.\",\"authors\":\"D Roelcke, A Leo, R Brossmer\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The Sia-lb1 epitope, recognized by anti-Sia-lb1 cold agglutinins, is unique since it is represented by the alpha-N-acetylneuraminic acid (alpha NeuNAc) monosaccharide. Chemical modifications of the chain at C-5 of alpha NeuNAc have shown that the natural 2-carbon and the artificial 3-carbon chains are optimal for anti-Sia-lb1 binding. Sia-lb1 antigenicity of alpha NeuNAc could be tenfold enhanced by replacement of the carbonyl oxygen by sulphur. The structural requirements of the Sia-lb1 epitope for optimal antibody binding were identified.</p>\",\"PeriodicalId\":79439,\"journal\":{\"name\":\"Beitrage zur Infusionstherapie und Transfusionsmedizin = Contributions to infusion therapy and transfusion medicine\",\"volume\":\"34 \",\"pages\":\"215-9\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1997-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Beitrage zur Infusionstherapie und Transfusionsmedizin = Contributions to infusion therapy and transfusion medicine\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Beitrage zur Infusionstherapie und Transfusionsmedizin = Contributions to infusion therapy and transfusion medicine","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Enhancement of Sia-lb1 antigenicity by sulphur-containing substituents at C-5 of free N-acetylneuraminic acid.
The Sia-lb1 epitope, recognized by anti-Sia-lb1 cold agglutinins, is unique since it is represented by the alpha-N-acetylneuraminic acid (alpha NeuNAc) monosaccharide. Chemical modifications of the chain at C-5 of alpha NeuNAc have shown that the natural 2-carbon and the artificial 3-carbon chains are optimal for anti-Sia-lb1 binding. Sia-lb1 antigenicity of alpha NeuNAc could be tenfold enhanced by replacement of the carbonyl oxygen by sulphur. The structural requirements of the Sia-lb1 epitope for optimal antibody binding were identified.