从牛脑中分离出与肌动蛋白丝具有不同亲和力的原肌球蛋白。

Isolation from bovine brain of tropomyosins that bind to actin filaments with different affinities.

作者信息

Keiser T, Wegner A

出版信息

FEBS Lett. 1985 Jul 22;187(1):76-80. doi: 10.1016/0014-5793(85)81218-7.

Abstract

Tropomyosin was isolated from bovine brain using mild conditions thereby avoiding heat precipitation. Separation by DEAE ion exchange chromatography yielded a 33 kDa tropomyosin and a mixture of 30 and 32 kDa tropomyosin. Binding of the tropomyosins to actin filaments was measured by a newly developed method. The binding was assayed by the retarding effect of tropomyosin on actin polymerization. The 33 kDa tropomyosin was found to bind to actin filaments with considerably higher affinity than the 30 and 32 kDa tropomyosin.

摘要

使用温和条件从牛脑中分离原肌球蛋白，从而避免热沉淀。通过DEAE离子交换色谱分离得到一种33 kDa的原肌球蛋白以及30 kDa和32 kDa原肌球蛋白的混合物。采用一种新开发的方法测定原肌球蛋白与肌动蛋白丝的结合。通过原肌球蛋白对肌动蛋白聚合的阻滞作用来测定结合情况。发现33 kDa的原肌球蛋白与肌动蛋白丝的结合亲和力明显高于30 kDa和32 kDa的原肌球蛋白。