PURIFICATION AND CHARACTERIZATION OF BOVINE HEART GLYCOGEN-SYNTHASE KINASE-3

被引：1
|
作者：
HENRY, SP
KILLILEA, SD
机构：
[1] Department of Biochemistry, North Dakota State University, Fargo, North Dakota
来源：
PREPARATIVE BIOCHEMISTRY | 1994年 / 24卷 / 3-4期
基金：
美国国家科学基金会;
关键词：
D O I：
10.1080/10826069408010098
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Glycogen Synthase Kinase-3 (GSK-3) was isolated from bovine heart tissue extracts by a procedure involving ammonium sulfate fractionation, followed by chromatography on phosphocellulose, Cibacron blue 3GA-agarose, DEAE-Sephacel, CM-Sepharose, heparin-agarose, myelin basic protein-Sepharose, and LiChrospher 1000 COO-. GSK-3 was identified by its activation of protein phosphatase-1(i) (PR-1(i)). The purified enzyme had a specific activity of 25,500 units of protein phosphatase-1(i) activated/mg protein. The enzyme is an asymmetric monomeric protein of 53 kDa. The molecular size and retention of activity after autophosphorylation indicated that the isolated enzyme was the GSK-3 alpha-isoform.
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页码：263 / 277
页数：15
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