首页    期刊浏览 2024年10月07日 星期一
登录注册

文章基本信息

  • 标题:Purification and Characterization of Silurus asotus (Catfish) Roe Lectin
  • 本地全文:下载
  • 作者:Masahiro HOSONO ; Hiroaki KAWAUCHI ; Kazuo NITTA
  • 期刊名称:Biological and Pharmaceutical Bulletin
  • 印刷版ISSN:0918-6158
  • 电子版ISSN:1347-5215
  • 出版年度:1993
  • 卷号:16
  • 期号:1
  • 页码:1-5
  • DOI:10.1248/bpb.16.1
  • 出版社:The Pharmaceutical Society of Japan
  • 摘要:A rhamnose-binding lectin isolated from Silurus asotus (catfish) roe by DEAE-cellulose ion exchange and galactose-Sepharose affinity chromatographies predominantly agglutinated human type B and rabbit erythrocytes. S. asotus lectin (SAL) also agglutinated sarcoma 180 ascites carcinoma cells, but not AH109A cells. The most effective saccharide in hemagglutination inhibition assay was L-rhamnose. The monosaccharides possessing steric similarity to the hydroxyl group orientation at C2 and C4 of the pyranose ring structure of L-rhamnose, such as L-mannose and L-lyxose, were also effective. The molecular weight of SAL was determined to be 38000 by size exclusion chromatography on TSK gel G3000SW and 33000 by SDS-polyacrylamide gel electrophoresis under reducing conditions. SAL did not require a Ca2+ ion or free thiol group for its agglutination activity. The N-terminal 29 amino acid sequence was determined by a gas-phase sequencer as follows, ANMITCYGDVQKLHXETGLIIVKSXLYGR (X : not determined). It has no homology to the sequences of well known vertebrate lectins.
  • 关键词:fish roe;rhamnose-binding lectin;affinity chromatography;N-terminal sequence
国家哲学社会科学文献中心版权所有