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

Authors: Moorhead, G  MacKintosh, C  Morrice, N  Cohen, P 
Citation: Moorhead G, etal., FEBS Lett. 1995 Apr 3;362(2):101-5.
Pubmed: (View Article at PubMed) PMID:7720853

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.


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RGD Object Information
RGD ID: 2304267
Created: 2009-03-12
Species: All species
Last Modified: 2009-03-12
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.