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：

加拿大自然科学与工程研究理事会; 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;

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.

引用

页码：101 / 105

页数：5

共 33 条

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