Purification of the hepatic glycogen‐associated form of protein phosphatase‐1 by microcystin‐Sepharose affinity chromatography

FEBS Letters

Moorhead, Greg¹  Morrice, Nick¹  MacKintosh, Carol¹  Cohen, Philip¹ 

[1] MRC Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, Dundee, DD1 4HN, Scotland, UK

关键词: Microcystin;    Protein phosphatase;    Glycogen;    Phosphorylase;    Glycogen synthase;   

DOI  :  10.1016/0014-5793(95)00197-H

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The form of protein phosphatase-1 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 α and β 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.

【 授权许可】

Unknown