从小麦胚芽中纯化和鉴定非依赖3',5'-磷酸腺苷的蛋白激酶
Purification and characterisation of adenosine-3',5'-phosphate-independent protein kinase from wheat germ.
作者信息
Rychlik W, Zagórski W
出版信息
Eur J Biochem. 1980 May;106(2):653-9. doi: 10.1111/j.1432-1033.1980.tb04613.x.
Abstract
cAMP-independent protein kinase was isolated from the wheat germ and purified to electrophoretic homogeneity. The molecular weight of enzyme was approximately 20,000, Km for ATP was (1 +/- 0.2) x 10(-5) M. V was 215 nmol phosphate mg enzyme-1 min-1, and the isoelectric point was at pH 9.2. The enzyme promotes phosphorylation of casein and crude wheat germ ribosomes.
摘要
不依赖环磷酸腺苷（cAMP）的蛋白激酶从小麦胚芽中分离出来，并纯化至电泳纯。该酶的分子量约为20,000，ATP的米氏常数（Km）为(1 +/- 0.2) x 10(-5) M。反应速度（V）为215 nmol磷酸/毫克酶/分钟，等电点为pH 9.2。该酶可促进酪蛋白和粗制小麦胚芽核糖体的磷酸化。
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