LeVine H, Sahyoun N, McConnell R, Bronson D, Cuatrecasas P
Biochem Biophys Res Commun. 1984 Jan 13;118(1):278-83. doi: 10.1016/0006-291x(84)91097-0.
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.
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。
