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聚合肌动蛋白水解ATP的机制。

The mechanism of ATP hydrolysis by polymer actin.

作者信息

Wegner A

出版信息

Biophys Chem. 1977 Jun;7(1):51-8. doi: 10.1016/0301-4622(77)87014-2.

Abstract

The rate of actin polymerization, the rate of nucleotide splitting and the rate of the nucleotide exchange have been measured simultaneously. Correlation of these three measurements demonstrated that nucleotide splitting and exchange were mainly connected with the association and dissociation reactions of actin protomers at the ends of actin filaments and were not caused by release and rebinding of nucleotide molecules at the binding sites along the filament. The observation made by others that the nucleotide exchange was accelerated in the presence of ATP was explained by the translocational head-to-tail polymerization of actin: Due to the simultaneous lengthening of the filament at one end and shortening at the other, nucleotide molecules are incorporated at one end and released at the other. In the absence of ATP, where the head-to-tail polymerization mechanism was not operative nucleotide exchange was brought about by the slow process of length fluctuation of polymers.

摘要

已同时测量了肌动蛋白聚合速率、核苷酸裂解速率和核苷酸交换速率。这三项测量结果的相关性表明,核苷酸裂解和交换主要与肌动蛋白原纤维在肌动蛋白丝末端的缔合和解离反应有关,而不是由核苷酸分子沿着丝在结合位点的释放和重新结合引起的。其他人观察到在ATP存在下核苷酸交换加速,这是由肌动蛋白的头对尾平移聚合来解释的:由于丝的一端同时延长而另一端缩短,核苷酸分子在一端掺入而在另一端释放。在没有ATP的情况下,头对尾聚合机制不起作用,核苷酸交换是由聚合物长度波动的缓慢过程引起的。

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