作者: D Blanchard , F Piller , B Gillard , D Marcus , J P Cartron
DOI: 10.1016/S0021-9258(17)39523-6
关键词: Sialoglycoproteins 、 Protease 、 Chemistry 、 Glycolipid 、 Biochemistry 、 Hemagglutination 、 Antibody 、 Ganglioside 、 Lectin 、 Antigen 、 Cell biology 、 Molecular biology
摘要: The blood group Cad antigen is a carbohydrate structure well characterized on the sialoglycoproteins of red cell membrane from some rare individuals (Blanchard, D., Cartron, J. P., Fournet, B., Montreuil, J., Van Halbeck, H., and Vliegenthart, J.F.G. (1983) Biol. Chem. 258, 7691-7695). However, protease treatment whole cells did not destroy their antigenic activity which indicated that glycolipid might also be involved in reaction. A crude ganglioside fraction was prepared found to inhibit hemagglutination reaction, whereas neutral glycolipids were inactive. Further analysis extract erythrocytes by thin layer chromatography revealed an unusual profile lower content sialosylparagloboside presence novel slower mobility. Immunochemical studies demonstrate this binds Helix pomatia lectin inhibits human anti-Sda antibody. In addition, with identical chromatographic mobility can obtained enzymatic transfer GalNAc UDP-GalNAc using microsomal preparation kidney. These results together surface labeling experiments suggest major derived substitution additional N-acetylgalactosamine residue.