Watanabe S, Maruyama K
Department of Biology, Faculty of Science, Chiba University.
J Biochem. 1993 Aug;114(2):181-5. doi: 10.1093/oxfordjournals.jbchem.a124152.
During a survey of actin pointed end-capping protein in salt extracts of rabbit skeletal muscle, it was found that native tropomyosin (troponin-tropomyosin complex) inhibited the seed activity of beta-actinin-capped actin filaments for actin polymerization. It turned out that beta-actinin-capped actin fragments reannealed to form long filaments resulting in the decrease in seed numbers in the presence of troponin and tropomyosin. It appears that the reannealing of actin filaments was due to release of beta-actinin from the actin filaments by troponin and tropomyosin. Either troponin or tropomyosin alone was not effective at all. Addition of an excess amount of beta-actinin did not prevent the reannealing of beta-actinin-capped actin filaments in the presence of troponin and tropomyosin.
在对兔骨骼肌盐提取物中的肌动蛋白尖端封端蛋白进行的一项研究中,发现天然原肌球蛋白(肌钙蛋白 - 原肌球蛋白复合物)抑制了β - 辅肌动蛋白封端的肌动蛋白丝对肌动蛋白聚合的种子活性。结果表明,在肌钙蛋白和原肌球蛋白存在的情况下,β - 辅肌动蛋白封端的肌动蛋白片段重新退火形成长丝,导致种子数量减少。似乎肌动蛋白丝的重新退火是由于肌钙蛋白和原肌球蛋白将β - 辅肌动蛋白从肌动蛋白丝上释放出来。单独的肌钙蛋白或原肌球蛋白根本没有效果。在肌钙蛋白和原肌球蛋白存在的情况下,添加过量的β - 辅肌动蛋白并不能阻止β - 辅肌动蛋白封端的肌动蛋白丝的重新退火。