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

Greg Moorhead, Carol MacKintosh, Nick Morrice, Philip Cohen

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    Abstract

    The form of protein phosphatase-l 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 (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.

    Original languageEnglish
    Pages (from-to)101-105
    Number of pages5
    JournalFEBS Letters
    Volume362
    Issue number2
    Publication statusPublished - 1995

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