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FEBS Lett. 1995 Apr 3;362(2):101-5.

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

Author information

1
Department of Biochemistry, University of Dundee, Scotland, UK.

Abstract

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 alpha and beta isoforms) complexed to a 33 kDa glycogen-binding (GL) subunit. The GL 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.

PMID:
7720853
DOI:
10.1016/0014-5793(95)00197-h
[Indexed for MEDLINE]
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