Hotta K
J Supramol Struct. 1975;3(4):333-7. doi: 10.1002/jss.400030404.
Myosin catalyzed exchange between 32Pi and ATP in reaction medium during its enzymatic hydrolysis of ATP only by a very small amount. Addition of actin increased to a great extent the rate of incorporation of 32Pi in the presence of Mg. Glycerinated smooth muscle fibers also exhibited the ability to exchange 32Pi and ATP upon the application of external force (repeated stretching and releasing). A schematic mechanism of the action of actin and external force on acceleration of 32Pi incorporation is proposed and the importance of the M-ADP complex for force generation is suggested.
肌球蛋白在其催化ATP酶促水解反应过程中，仅使反应介质中32Pi与ATP之间发生极少量的交换。添加肌动蛋白后，在镁离子存在的情况下，32Pi掺入速率大幅增加。甘油化的平滑肌纤维在施加外力（反复拉伸和释放）时，也表现出32Pi与ATP交换的能力。本文提出了肌动蛋白和外力加速32Pi掺入作用的示意机制，并指出了M-ADP复合物对力产生的重要性。
