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三乙铅离子(Et3Pb+)与微管蛋白相互作用的分子机制。

The molecular mechanism of interaction of Et3Pb+ with tubulin.

作者信息

Faulstich H, Stournaras C, Doenges K H, Zimmermann H P

出版信息

FEBS Lett. 1984 Aug 20;174(1):128-31. doi: 10.1016/0014-5793(84)81090-x.

Abstract

Triethyllead ion (Et3Pb+) was found to interact with 2 out of 18 thiol groups present in tubulin dimers. Specificity of the interaction was shown by the high affinity of Et3Pb+ to tubulin, by the fact that the 16 residual thiol groups in tubulin remained unaffected, and by the observation that other proteins with exposed thiol groups, e.g., actin, did not react with Et3Pb+. After complexation of the two thiol groups, tubulin in vitro had lost its capability for microtubule assembly. Likewise, polymerized tubulin disassembled on addition of the lead compound.

摘要

已发现三乙基铅离子(Et3Pb+)与微管蛋白二聚体中18个巯基中的2个发生相互作用。Et3Pb+与微管蛋白的高亲和力、微管蛋白中16个残留巯基未受影响这一事实以及观察到其他具有暴露巯基的蛋白质(如肌动蛋白)不与Et3Pb+反应,均表明了这种相互作用的特异性。两个巯基络合后,体外微管蛋白失去了微管组装能力。同样,添加铅化合物后,聚合的微管蛋白会解聚。

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