Porter M E, Johnson K A
J Submicrosc Cytol. 1983 Jan;15(1):199-200.
The binding of Tetrahymena 30S dynein to bovine brain microtubules has been examined. The dynein was bound by its B-end or ATP sensitive site with a stoichiometry of 1 dynein arm per 6 tubulin dimers. Addition of ATP released virtually all the dynein from the surface of the microtubule. Following hydrolysis of the ATP, the dynein reassociated with the microtubule.
已经对嗜热四膜虫30S动力蛋白与牛脑微管的结合进行了研究。动力蛋白通过其B端或ATP敏感位点结合,化学计量比为每6个微管蛋白二聚体有1个动力蛋白臂。添加ATP后,几乎所有动力蛋白都从微管表面释放出来。ATP水解后,动力蛋白重新与微管结合。