首页    期刊浏览 2024年12月01日 星期日
登录注册

文章基本信息

  • 标题:Interactions of a photoaffinity analog of GTP with the proteins of microtubules
  • 本地全文:下载
  • 作者:R L Geahlen ; B E Haley
  • 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:1977
  • 卷号:74
  • 期号:10
  • 页码:4375-4377
  • DOI:10.1073/pnas.74.10.4375
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Tubulin dimers isolated from brain contain two GTP binding sites, a nonexchangeable site and an exchangeable site. To localize the exchangeable site, we used a photoaffinity analog of GTP, 8-azidoguanosine triphosphate (8-N3GTP), which supports tubulin polymerization in the absence of activating light. Photolysis of tubulin polymerized in the presence of 0.01 to 0.1 mM [beta, gamma-32P]8-N3GTP resulted in covalent incorporation of radioactivity only onto the beta monomer. Photolysis with 8-N3GTP also prevented any further repolymerization of the tubulin whereas like treatment in the presence of GTP had no effect. Preincubation of tubulin with GTP prevented photo-incorporation of [beta, gamma-32P]8-N3GTP whereas preincubation with ATP did not.
国家哲学社会科学文献中心版权所有