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一种磷脂磷酸酶对Ca2+依赖性蛋白激酶磷酸化组蛋白H1的特异性存在于催化亚基中。

Specificity of a phosphatase for phospholipid, Ca2+-dependent protein kinase-phosphorylated histone H1 resides in the catalytic subunit.

作者信息

LeVine H, Sahyoun N, McConnell R, Bronson D, Cuatrecasas P

出版信息

Biochem Biophys Res Commun. 1984 Jan 13;118(1):278-83. doi: 10.1016/0006-291x(84)91097-0.

Abstract

A protein phosphatase from liver which acts preferentially on histone phosphorylated with phospholipid, Ca2+-dependent protein kinase has been purified and the intrinsic specificity determined to reside in the catalytic subunit of the enzyme complex. Comparison with a preparation of pork heart protein phosphatase suggests that this specificity may be a general property of a class of protein phosphatases. Protein kinase C-phosphorylated histone H1 represents an improved substrate for phosphatase detection providing a five to tenfold greater sensitivity than other substrates including cAMP-dependent protein kinase phosphorylated H1.

摘要

一种来自肝脏的蛋白磷酸酶已被纯化,该酶优先作用于由磷脂、Ca2+依赖性蛋白激酶磷酸化的组蛋白,其内在特异性被确定存在于酶复合物的催化亚基中。与猪心蛋白磷酸酶制剂的比较表明,这种特异性可能是一类蛋白磷酸酶的普遍特性。蛋白激酶C磷酸化的组蛋白H1是用于磷酸酶检测的改良底物,与包括cAMP依赖性蛋白激酶磷酸化的H1在内的其他底物相比,其灵敏度提高了五到十倍。

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