Kanoh H, Ono T
FEBS Lett. 1986 May 26;201(1):97-100. doi: 10.1016/0014-5793(86)80577-4.
Pig brain diacylglycerol kinase did not catalyze autophosphorylation. However, the kinase was phosphorylated on serine, when immunoprecipitated from the partially purified enzyme preparation preincubated with Mg2+ and [gamma-32P]ATP. The action of the endogenous protein kinase phosphorylating diacylglycerol kinase was independent of cyclic nucleotides and Ca2+, and became maximum at pH 5.5. Although the extent of enzyme phosphorylation was limited (maximally about 0.25 mol Pi incorporated per mol kinase), the results show that diacylglycerol kinase can be a phosphoprotein.
猪脑二酰基甘油激酶不催化自身磷酸化。然而,当从与Mg2+和[γ-32P]ATP预孵育的部分纯化酶制剂中进行免疫沉淀时,该激酶在丝氨酸上被磷酸化。内源性蛋白激酶使二酰基甘油激酶磷酸化的作用不依赖于环核苷酸和Ca2+,并且在pH 5.5时达到最大值。尽管酶磷酸化的程度有限(每摩尔激酶最多掺入约0.25摩尔磷酸根离子),但结果表明二酰基甘油激酶可以是一种磷蛋白。