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Purification of the hepatic glycogen‐associated form of protein phosphatase‐1 by microcystin‐Sepharose affinity chromatography
Author(s) -
Moorhead Greg,
MacKintosh Carol,
Morrice Nick,
Cohen Philip
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00197-h
Subject(s) - glycogen phosphorylase , affinity chromatography , protein phosphatase 1 , phosphorylase kinase , protein subunit , biochemistry , sepharose , dephosphorylation , glycogen synthase , allosteric regulation , phosphatase , size exclusion chromatography , chemistry , enzyme , glycogen , microbiology and biotechnology , biology , gene
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 .