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

Greg Moorhead, Carol MacKintosh, Nick Morrice, Philip Cohen

    Research output: Contribution to journalArticle

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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

    Cite this

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    title = "Purification of the hepatic glycogen-associated form of protein phosphatase-1 by microcystin-Sepharose affinity chromatography",
    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.",
    author = "Greg Moorhead and Carol MacKintosh and Nick Morrice and Philip Cohen",
    year = "1995",
    language = "English",
    volume = "362",
    pages = "101--105",
    journal = "FEBS Letters",
    issn = "0014-5793",
    publisher = "Wiley",
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    Purification of the hepatic glycogen-associated form of protein phosphatase-1 by microcystin-Sepharose affinity chromatography. / Moorhead, Greg; MacKintosh, Carol; Morrice, Nick ; Cohen, Philip.

    In: FEBS Letters, Vol. 362, No. 2, 1995, p. 101-105.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - Purification of the hepatic glycogen-associated form of protein phosphatase-1 by microcystin-Sepharose affinity chromatography

    AU - Moorhead, Greg

    AU - MacKintosh, Carol

    AU - Morrice, Nick

    AU - Cohen, Philip

    PY - 1995

    Y1 - 1995

    N2 - 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.

    AB - 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.

    M3 - Article

    VL - 362

    SP - 101

    EP - 105

    JO - FEBS Letters

    JF - FEBS Letters

    SN - 0014-5793

    IS - 2

    ER -