PURIFICATION OF THE HEPATIC GLYCOGEN-ASSOCIATED FORM OF PROTEIN PHOSPHATASE-1 BY MICROCYSTIN-SEPHAROSE AFFINITY-CHROMATOGRAPHY

被引：84
作者：
MOORHEAD, G
MACKINTOSH, C
MORRICE, N
COHEN, P
机构：
[1] MRC Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, Dundee
来源：
FEBS LETTERS | 1995年 / 362卷 / 02期
基金：
英国医学研究理事会; 英国生物技术与生命科学研究理事会; 加拿大自然科学与工程研究理事会;
关键词：
MICROCYSTIN; PROTEIN PHOSPHATASE; GLYCOGEN; PHOSPHORYLASE; GLYCOGEN SYNTHASE;
D O I：
10.1016/0014-5793(95)00197-H
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：
The form of protein phosphatase-l associated with hepatic glycogen (PP1G) was purified to near homogeneity from rat liver by affinity chromatography on microcystin-Sepharose and gel-filtration, The enzyme is a heterodimer consisting of the catalytic subunit of PP1 (the alpha and beta isoforms) complexed to a 33 kDa glycogen-binding (G(L)) subunit. The G(L) subunit binds phosphorylase a with high affinity, and is responsible for the enhanced dephosphorylation of glycogen synthase by PP1G and its allosteric inhibition by phosphorylase a.
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页码：101 / 105
页数：5
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