Nakashima M, Takai Y, Yamamura H, Nishizuka Y
Biochim Biophys Acta. 1975 Jul 27;397(1):117-23. doi: 10.1016/0005-2744(75)90185-0.
A protein kinase (ATP: protein phosphotransferase, EC 2.7.1.37) which preferentially phosphorylates protamine is purified about 250-fold from the soluble fraction of baker's yeast (Saccharomyces cerevisiae). This enzyme is not sensitive to activation by cyclic nucleotides. Histone is about 5% as active as protamine in the reaction rate. Neither casein, phosvitin nor glycogen phosphorylase is active as substrate. The enzyme is distinguishable from casein kinase of the classical type (Rabinowitz, M. and Lipmann, F. (1960) J. Biol. Chem. 235, 1043-1050) and from adenoshine 3', 5'-monophosphate-dependent protein kinase described earlier (Takai, Y., Yamamura, H. and Nishizuka, Y. (1974) J. Biol. Chem. 249,530-535).
一种优先使鱼精蛋白磷酸化的蛋白激酶（ATP：蛋白磷酸转移酶，EC 2.7.1.37）从面包酵母（酿酒酵母）的可溶性部分中纯化出来，纯化倍数约为250倍。这种酶对环核苷酸的激活不敏感。在反应速率方面，组蛋白的活性约为鱼精蛋白的5%。酪蛋白、卵黄高磷蛋白和糖原磷酸化酶作为底物均无活性。该酶与经典类型的酪蛋白激酶（拉比诺维茨，M.和利普曼，F.（1960年）《生物化学杂志》235卷，1043 - 1050页）以及先前描述的3'，5'-单磷酸腺苷依赖性蛋白激酶（高井，Y.、山村，H.和西冢，Y.（1974年）《生物化学杂志》249卷，530 - 535页）不同。
