Yang S D, Vandenheede J R, Merlevede W
Biochem Biophys Res Commun. 1984 Feb 14;118(3):923-8. doi: 10.1016/0006-291x(84)91483-9.
A high molecular weight protein phosphatase (Mr = 260K) has been isolated from rabbit skeletal muscle. The enzyme has a very low activity towards phosphorylase a isolated from the same tissue, but its activity towards this substrate is stimulated several fold after dissociation by 2-mercaptoethanol treatment. The purified phosphatase shows one major protein staining band on non denaturing polyacrylamide gel electrophoresis, and contains four subunits with molecular weights of 95K, 75K, 65K and 38K. The catalytic activity resides in the Mr = 38K subunit and is not sensitive to inhibition by the heat stable protein phosphatase inhibitor-1 or modulator protein. Polyamines stimulate the holoenzyme in a dose dependent, biphasic manner, but inhibit the activity of the dissociated Mr = 38K catalytic subunit.
一种高分子量蛋白磷酸酶（Mr = 260K）已从兔骨骼肌中分离出来。该酶对从同一组织中分离出的磷酸化酶a的活性非常低，但经2-巯基乙醇处理解离后，其对该底物的活性会被刺激数倍。纯化后的磷酸酶在非变性聚丙烯酰胺凝胶电泳上显示出一条主要的蛋白染色带，并包含四个分子量分别为95K、75K、65K和38K的亚基。催化活性存在于Mr = 38K的亚基中，对热稳定蛋白磷酸酶抑制剂-1或调节蛋白的抑制不敏感。多胺以剂量依赖性的双相方式刺激全酶，但抑制解离后的Mr = 38K催化亚基的活性。
