Tusupov O K, Severin S E, Shvets V I
M.V. Lomonosov Institute of Fine Chemical Technology, Moscow, USSR.
Biochem Biophys Res Commun. 1991 May 15;176(3):1007-13. doi: 10.1016/0006-291x(91)90382-h.
Limited tryptic proteolysis of homogeneous protein kinase C induces the formation of a catalytically active fragment of 50 kDa (kinase M) which, unlike native PK C acquires the ability to phosphorylate PIP. Both ATP and GTP were found to be capable of serving as phosphate donors in this process. Incubation of purified kinase M with a preparation of rat brain membrane fraction enhanced the level of phosphorylation of PIP in the presence and in the absence of exogenous PIP. A scheme of the interrelationship of phosphoinositide metabolism and the proteolytic processing of protein kinase C is proposed.
对均一的蛋白激酶C进行有限的胰蛋白酶解，可诱导形成一个50 kDa的具有催化活性的片段（激酶M），与天然蛋白激酶C不同的是，它获得了磷酸化磷脂酰肌醇（PIP）的能力。在此过程中，发现ATP和GTP都能够作为磷酸供体。在有或没有外源性PIP存在的情况下，将纯化的激酶M与大鼠脑膜部分制剂一起孵育，可提高PIP的磷酸化水平。本文提出了磷酸肌醇代谢与蛋白激酶C蛋白水解加工之间相互关系的示意图。
