原肌球蛋白抑制F-肌动蛋白和细丝蛋白的相互作用。
Tropomyosin inhibits the interaction of F-actin and filamin.
作者信息
Maruyama K, Ohashi K
出版信息
J Biochem. 1978 Oct;84(4):1017-9. doi: 10.1093/oxfordjournals.jbchem.a132184.
Abstract
The value of flow birefringence of F-actin was greatly decreased by filamin due to precipitate formation. This precipitate could be dispersed into birefringent filaments by sonication. Tropomyosin inhibited precipitation of F-actin induced by filamin, and no decrease in birefringence occurred when filamin was added to tropomyosin-bound F-actin. Hence it appears that filamin acts on F-actin in non-muscle cells similarly to alpha-actinin.
摘要
由于沉淀形成，细丝蛋白极大地降低了F - 肌动蛋白的流动双折射值。这种沉淀可通过超声处理分散成双折射细丝。原肌球蛋白抑制细丝蛋白诱导的F - 肌动蛋白沉淀，当将细丝蛋白添加到与原肌球蛋白结合的F - 肌动蛋白中时，双折射没有降低。因此，细丝蛋白在非肌肉细胞中对F - 肌动蛋白的作用似乎与α - 辅肌动蛋白类似。
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