大鼠肝脏核蛋白激酶的分级分离与部分纯化

Fractionation and partial purification of rat liver nuclear protein kinases.

作者信息

Goueli S A, Ahmed K

出版信息

Int J Biochem. 1983;15(9):1109-18. doi: 10.1016/0020-711x(83)90225-2.

Abstract

We have fractional and partially purified several rat liver nuclear protein kinases by utilizing endogenous (nonhistone proteins) and exogenous acidic (dephosphophosvitin) and basic (lysine-rich histone) protein substrates. Three enzymes were active towards endogenous substrates, two towards dephosphophosvitin and two towards lysine-rich histone. Of the latter only one was cAMP-dependent, however, only minimal cAMP binding activity was detected. Several features of these enzyme reactions are described revealing distinct differences in the characteristics of each of these enzymes.

摘要

我们利用内源性（非组蛋白）、外源性酸性（脱磷酸磷卵黄蛋白）和碱性（富含赖氨酸的组蛋白）蛋白质底物，对几种大鼠肝脏核蛋白激酶进行了分级分离和部分纯化。三种酶对内源性底物有活性，两种对脱磷酸磷卵黄蛋白有活性，两种对富含赖氨酸的组蛋白有活性。在后者中只有一种是cAMP依赖性的，然而，仅检测到最小的cAMP结合活性。描述了这些酶反应的几个特征，揭示了每种酶特性的明显差异。