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原肌球蛋白重叠的消除以及肌动蛋白亚片段-1 ATP 酶对钙离子浓度增加的协同反应。

Removal of tropomyosin overlap and the co-operative response to increasing calcium concentrations of the acto-subfragment-1 ATPase.

作者信息

Walsh T P, Trueblood C E, Evans R, Weber A

出版信息

J Mol Biol. 1985 Mar 20;182(2):265-9. doi: 10.1016/0022-2836(85)90344-4.

Abstract

The co-operative response of regulated actomyosin ATPase to increasing concentrations of calcium has been attributed to nearest-neighbor interactions, presumably between troponin-tropomyosin complexes. The degree of co-operativity was not decreased after the carboxy-terminal 11 amino acid residues had been removed from tropomyosin by carboxypeptidase A. This indicates that the interactions between neighboring troponin-tropomyosin complexes do not occur through the overlapping tropomyosin ends.

摘要

调节型肌动球蛋白ATP酶对钙浓度升高的协同反应归因于最近邻相互作用,推测是在肌钙蛋白-原肌球蛋白复合物之间。在用羧肽酶A从原肌球蛋白上去除羧基末端的11个氨基酸残基后,协同程度并未降低。这表明相邻肌钙蛋白-原肌球蛋白复合物之间的相互作用不是通过重叠的原肌球蛋白末端发生的。

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