Toyoshima Y Y
Department of Biology, Ochanomizu University, Tokyo, Japan.
J Cell Sci Suppl. 1991;14:83-5. doi: 10.1242/jcs.1991.supplement_14.17.
Flexibility of the myosin molecule was studied by an in vitro motility assay in terms of the direction of actin movement. Actin filaments can move in both directions on tracks of heavy meromyosin made on a nitrocellulose surface, and, furthermore, along the native thick filaments passing over their central bare zone. These observations indicate that the myosin molecule has a considerable flexibility in interacting with actin filaments.
通过体外运动分析,依据肌动蛋白的运动方向对肌球蛋白分子的柔韧性进行了研究。肌动蛋白丝能够在硝酸纤维素表面形成的重酶解肌球蛋白轨道上双向移动,此外,还能沿着穿过其中心裸区的天然粗肌丝移动。这些观察结果表明,肌球蛋白分子在与肌动蛋白丝相互作用时具有相当大的柔韧性。