| Literature DB >> 7720853 |
G Moorhead1, C MacKintosh, N Morrice, P Cohen.
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.Entities:
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Year: 1995 PMID: 7720853 DOI: 10.1016/0014-5793(95)00197-h
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124