Relationships between dephosphorylation and D to I conversion of rabbit skeletal muscle glycogen synthase

B. S. Khatra, T. R. Soderling

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    12 Scopus citations

    Abstract

    The relationship between dephosphorylation and D to I conversoon of skeletal muscle glycogen synthase by synthase phosphatase was investigated using synthase preparations containing 1 to 3 mol of 32P/mol of subunit (90,000 g). Dephosphorylation was analyzed in terms of 32P release from the trypsin-sensitive and trypsin-insensitive phosphorylation regions of synthase. With synthase containing 1 to 2 mol of 32P/90,000 g, dephosphorylation of the trypsin-insensitive region correlated closely with D to I conversion and was more rapid than dephosphorylation of the trypsin-sensitive region. Synthase containing 3 mol of 32P/90,000 g was a relatively poor substrate for the phosphatase since dephosphorylation of both regions, as well as D to I conversion, was slow. With this species of synthase, glucose-6-P (0.1 mM) increased the rates of D to I conversion and dephosphorylation of trypsin-insensitive region. It is concluded that dephosphorylation of the trypsin-insensitive region is responsible for the conversion of synthase D to I.

    Original languageEnglish (US)
    Pages (from-to)5247-5250
    Number of pages4
    JournalJournal of Biological Chemistry
    Volume253
    Issue number15
    StatePublished - 1978

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

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