Effect of phosphorylation on the actin-activated ATPase activity of myosin.
Effect of phosphorylation on the actin-activated ATPase activity of myosin.
复制标题
磷酸化对肌球蛋白肌动蛋白激活的 ATP 酶活性的影响。
DOI：
10.1016/0006-291x(81)91182-7
复制
发表时间：
1981
影响因子：
3.1
通讯作者：
Hartshorne,DJ
中科院分区：
文献类型：
--
作者：
Persechini,A;Mrwa,U;Hartshorne,DJ
本研究旨在验证肌球蛋白磷酸化是肌球蛋白Mg ~（2+）-ATP酶活性激活的唯一原因这一假说。使用洗涤的天然肌动球蛋白和重构的肌动球蛋白，结果表明，磷酸化单独引起ATP酶活性的轻微激活。只有当加入除肌球蛋白轻链激酶外的蛋白质时才能获得完全活性。从这些结果可以明显看出：1）肌球蛋白磷酸化的程度与肌动球蛋白的特异性Mg ~（2+）-ATP酶活性之间没有简单的关系; 2）为了使磷酸化肌球蛋白的Mg ~（2+）-ATP酶活性被肌动蛋白完全激活，需要额外的因子。
The purpose of this study was to test the hypothesis that the phosphorylation of myosin is solely responsible for the activation of the Mg2+-ATPase activity of gizzard actomyosin. Using a washed natural actomyosin and a reconstituted actomyosin it was shown that phosphorylation alone caused only a slight activation of ATPase activity. Full activity was obtained only when proteins in addition to the myosin light chain kinase were added. It is evident from these results that: 1) there is no simple relationship between the extent of myosin phosphorylation and the specific Mg2+-ATPase activity of actomyosin and 2) in order for full activation by actin of the Mg2+-ATPase activity of phosphorylated myosin additional factors are required.