Elliott D C, Kokke Y S
Biochem Biophys Res Commun. 1987 Jun 30;145(3):1043-7. doi: 10.1016/0006-291x(87)91541-5.
The partly purified calcium-dependent, phospholipid-activated protein kinase from A. tricolor seedlings contains three major protein species (Mr = 84,500, 65,000 and 40,000) which cross-react with antiserum raised against the regulatory domain of bovine brain protein kinase C. Two of these species (Mr = 84,500 and 40,000) were phosphorylated when the preparation was incubated with [gamma-32P] ATP. It is suggested that the three cross-reacting proteins correspond to native enzyme, partly proteolysed enzyme and regulatory sub-unit respectively.
从三色苋幼苗中部分纯化得到的钙依赖性磷脂激活蛋白激酶含有三种主要蛋白质（分子量分别为84,500、65,000和40,000），它们与针对牛脑蛋白激酶C调节结构域产生的抗血清发生交叉反应。当该制剂与[γ-32P]ATP一起孵育时，其中两种蛋白质（分子量分别为84,500和40,000）发生了磷酸化。有人提出，这三种交叉反应蛋白分别对应于天然酶、部分蛋白酶解的酶和调节亚基。
