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  • 标题:Galactosyltransferase and Concanavalin A Agglutination of Cells
  • 本地全文:下载
  • 作者:Daniel K. Podolsky ; Milton M. Weiser ; J. Thomas La Mont
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1974
  • 卷号:71
  • 期号:3
  • 页码:904-908
  • DOI:10.1073/pnas.71.3.904
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:A correlation has been observed between concanavalin A agglutination of various cell types and the presence of surface membrane galactosyltransferase (1-O-[α]-D-Galactosyl-myo-inositol:raffinose galactosyltransferase, EC 2.4.1.67 ) activity. Moreover, a reduction to less than 50% of cell surface galactosyltransferase activity occurred after treatment with concanavalin A; other cell surface glycosyltransferase enzyme activities examined were unaffected by concanavalin A treatment. To confirm the participation of cell surface galactosyltransferase in concanavalin A-induced cell agglutination, the enzyme from rabbit erythrocytes was solubilized by sonication and purified by preparative polyacrylamide gel electrophoresis. It was possible to achieve a purified preparation of rabbit erythrocyte galactosyltransferase by separation on concanavalin A-Sepharose. The purified enzyme showed visible immunoprecipitation (Ouchterlony) with concanavalin A. Furthermore, human erythrocytes, which are not normally agglutinated by concanavalin A, became agglutinable by the lectin when the erythrocytes were preincubated with purified galactosyltransferase. These experiments suggest a direct and possible specific role of cell surface galactosyltransferase enzyme in the mechanism of concanavalin A agglutination of cells.
  • 关键词:lectin ; erythrocytes ; cell surface enzyme
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