Reisler E
J Biol Chem. 1980 Oct 25;255(20):9541-4.
The kinetic properties of actomyosin have been examined using complexes of actin with the recently described (Reisler, E., Smith, C., and Seegan, G. (1980) J. Mol. Biol., in press) short, bipolar synthetic myosin filaments (minifilaments). It is shown, in contrast to previous observations with aggregated and insoluble myosin, that the kinetic behavior of actomyosin is similar to that of acto-heavy meromyosin. Owing to their size, solubility, and stability under conditions of the actin-activated ATPase measurements, the minifilaments provide a well defined experimental system. Thus, they constitute a convenient and appropriate material for studying actomyosin interactions.
利用肌动蛋白与最近描述的（雷斯勒，E.，史密斯，C.，和西根，G.（1980年）《分子生物学杂志》，即将发表）短的、双极合成肌球蛋白丝（微丝）形成的复合物，对肌动球蛋白的动力学特性进行了研究。结果表明，与先前对聚集的和不溶性肌球蛋白的观察结果相反，肌动球蛋白的动力学行为与肌动蛋白-重酶解肌球蛋白的相似。由于微丝的大小、溶解性以及在肌动蛋白激活的ATP酶测量条件下的稳定性，它们提供了一个定义明确的实验系统。因此，它们构成了研究肌动球蛋白相互作用的方便且合适的材料。
