从大鼠脑中分离出的起始因子2含有负责其磷酸化的激酶活性。

Initiation factor 2 isolated from rat brain contains kinase activities responsible for its phosphorylation.

作者信息

Calés C, Fando J L, Fernández T, Alcázar A, Salinas M

出版信息

Neurosci Lett. 1985 Nov 11;61(3):333-7. doi: 10.1016/0304-3940(85)90486-0.

DOI:10.1016/0304-3940(85)90486-0

Abstract

Initiation factor 2 from adult rat brain was isolated from salt-washed microsomes using a three-step purification process consisting of heparin-Sepharose, phosphocellulose and diethylaminoethyl-cellulose (DEAE cellulose) column chromatographies. The initiation factor 2(eIF-2) was phosphorylated in subunits alpha and beta by the endogenous protein kinase activity present in the pruified preparation. This protein kinase activity proved to be mostly a casein kinase, although the possible presence of a very specific alpha kinase activity cannot be dismissed.

摘要

采用三步纯化法从盐洗微粒体中分离成年大鼠脑起始因子2，该方法包括肝素-琼脂糖、磷酸纤维素和二乙氨基乙基纤维素（DEAE纤维素）柱色谱法。纯化制剂中存在的内源性蛋白激酶活性使起始因子2（eIF-2）的α和β亚基发生磷酸化。尽管不能排除非常特异的α激酶活性的可能存在，但这种蛋白激酶活性经证实主要是一种酪蛋白激酶。

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Initiation factor 2 isolated from rat brain contains kinase activities responsible for its phosphorylation.从大鼠脑中分离出的起始因子2含有负责其磷酸化的激酶活性。

Neurosci Lett. 1985 Nov 11;61(3):333-7. doi: 10.1016/0304-3940(85)90486-0.

2

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An improved purification procedure and properties of casein kinase II from brain.一种改进的从大脑中纯化酪蛋白激酶II的方法及其性质

Neurochem Res. 1988 Sep;13(9):829-36. doi: 10.1007/BF00970750.

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