Hayashi T
J Gen Physiol. 1967 Jul;50(6):Suppl:119-33. doi: 10.1085/jgp.50.6.119.
The molecular basis for the mechanism of contraction in striated muscle, with primary emphasis on the interaction between the thick and thin filaments and the role of the thin (actin) filaments, is the theme presented. Recent information relating to actin-myosin interaction points up the fact that definitive statements cannot be made regarding the molecular interaction(s) that lead to contraction. Nevertheless, the properties of actin indicate that (a) actin in the monomeric state has properties differing markedly from actin in the polymer (filament) state; (b) these property differences may be significant in the contractile process, for they include changes in the reactivity of the bound nucleotide and actin-myosin complex formation; (c) the bound nucleotide seems to be required in the contraction process. For these, and other, reasons discussed, the tentative hypothesis is advanced that the contraction reaction involves local changes in the actin filament providing local monomer or monomer-like actin units in the reaction with myosin.
本文介绍的主题是横纹肌收缩机制的分子基础，主要强调粗肌丝和细肌丝之间的相互作用以及细（肌动蛋白）丝的作用。与肌动蛋白 - 肌球蛋白相互作用相关的最新信息表明，关于导致收缩的分子相互作用无法给出明确的陈述。然而，肌动蛋白的特性表明：（a）单体状态的肌动蛋白具有与聚合物（丝）状态的肌动蛋白明显不同的特性；（b）这些特性差异在收缩过程中可能很重要，因为它们包括结合核苷酸的反应性变化和肌动蛋白 - 肌球蛋白复合物的形成；（c）收缩过程似乎需要结合核苷酸。基于这些以及其他讨论的原因，提出了一个初步假设，即收缩反应涉及肌动蛋白丝的局部变化，在与肌球蛋白的反应中提供局部单体或类似单体的肌动蛋白单元。
