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  • 标题:In vitro assembly of pure tubulin into microtubules in the absence of microtubule-associated proteins and glycerol
  • 本地全文:下载
  • 作者:W Herzog ; K Weber
  • 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:5
  • 页码:1860-1864
  • DOI:10.1073/pnas.74.5.1860
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Microtubule protein from porcine cerebrum was fractionate into pure tubulin and microtubule-associated proteins by chromatography on phosphocellulose. In agreement with previous studies, pure tubulin does not form microtubules to a significant extent at 37 degrees in normal assembly buffers, which are characterized by a low concentration of Mg2+ ions. If, however, the Mg2+ concentration is raised to approximately 10 mM, rapid and extensive self-assembly of pure tubulin into microtubules is observed, provided the tubulin concentration is above 2.5 mg/ml. At a protein concentration of 3 mg/ml, the lag period is 1.5 min and the assembly process is virtually complete after 6 min at 37 degrees. These microtubules are like normal microtubules--sensitive to calcium ions, colchicine, and low temperature.
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