一种高度特异性蛋白激酶使酵母60S核糖体亚基的两种强酸性蛋白磷酸化的证据。
Evidence for a highly specific protein kinase phosphorylating two strongly acidic proteins of yeast 60 S ribosomal subunit.
作者信息
Kudlicki W, Szyszka R, Paleń E, Gasior E
出版信息
Biochim Biophys Acta. 1980 Dec 15;633(3):376-85. doi: 10.1016/0304-4165(80)90196-8.
PMID:7011390
Abstract
Two distinct, cyclic AMP-independent protein kinase (ATP : protein photransferase, EC 2.7.1.37) from yeast have been isolated and highly purified. The first of the enzymes, protein kinase 1 A, phosphorylates casein and phosvitin, and its cellular protein substrate is unknown. The second enzyme, protein kinase 1 B, phosphorylates two strongly acidic proteins, L44 and L45, of the 60 S ribosomal subunit.
摘要
已从酵母中分离并高度纯化出两种不同的、不依赖环磷酸腺苷的蛋白激酶（ATP：蛋白质磷酸转移酶，EC 2.7.1.37）。第一种酶，蛋白激酶1A，可使酪蛋白和卵黄高磷蛋白磷酸化，其细胞内蛋白质底物尚不清楚。第二种酶，蛋白激酶1B，可使60S核糖体亚基的两种强酸性蛋白L44和L45磷酸化。
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