Verkhovskiĭ A B, Surgucheva I G, Gel'fand V I
Mol Biol (Mosk). 1986 Jul-Aug;20(4):929-35.
Functional properties of the protein complex from bovine brain that shortens actin filaments are described. In the presence of Ca2+ complex shortens actin filaments and increases the initial rate of actin polymerization. In the absence of free calcium ions the complex loses its accelerating effect on actin polymerization, but still possesses actin filament shortening activity. Neither phalloidin nor tropomyosin prevent the shortening of actin filaments induced by the protein complex. Therefore the protein complex causes the fragmentation of actin filament. The data on actin polymerization in the presence of F-actin nuclei have indicated that the protein complex inhibits the elongation step of actin polymerization. The analysis of elongation in the presence of both the protein complex and cytochalasin D has demonstrated that the inhibition occurs on the fast-growing end of actin filaments.
描述了来自牛脑的能使肌动蛋白丝缩短的蛋白质复合物的功能特性。在Ca2+存在的情况下，该复合物会缩短肌动蛋白丝并提高肌动蛋白聚合的初始速率。在没有游离钙离子的情况下，该复合物失去了对肌动蛋白聚合的加速作用，但仍具有肌动蛋白丝缩短活性。鬼笔环肽和原肌球蛋白均不能阻止该蛋白质复合物诱导的肌动蛋白丝缩短。因此，该蛋白质复合物导致肌动蛋白丝断裂。在F-肌动蛋白核存在的情况下关于肌动蛋白聚合的数据表明，该蛋白质复合物抑制肌动蛋白聚合的延伸步骤。在蛋白质复合物和细胞松弛素D同时存在的情况下对延伸的分析表明，抑制发生在肌动蛋白丝的快速生长末端。
