一种分离兔网织红细胞血红素控制的真核起始因子2α蛋白激酶的新方法。
A novel approach to the isolation of rabbit reticulocyte haem-controlled eIF-2 alpha protein kinase.
作者信息
Jackson R J, Hunt T
出版信息
Biochim Biophys Acta. 1985 Dec 18;826(4):224-8. doi: 10.1016/0167-4781(85)90010-7.
PMID:4074745
Abstract
A new strategy for the purification of rabbit reticulocyte haem-controlled eIF-2 alpha kinase is described, based on the fact that this kinase can be self-phosphorylated in several sites. Incubation of partially purified kinase with ATP changes its behaviour on anion exchangers sufficiently to separate it from almost all contaminating proteins.
摘要
基于兔网织红细胞血红素控制的真核起始因子2α激酶（eIF-2α激酶）能在多个位点进行自我磷酸化这一事实，本文描述了一种纯化该激酶的新策略。将部分纯化的激酶与ATP一起温育，足以改变其在阴离子交换剂上的行为，从而将其与几乎所有污染蛋白分离。
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