Glycogen synthetase kinase 2 and adenosine 3'

5' cyclic monophosphate independent protein kinase activities in rabbit skeletal muscle

H. G. Nimmo, P. Cohen

    Research output: Contribution to journalArticle

    2 Citations (Scopus)

    Abstract

    The major phosvitin kinase activity in skeletal muscle is distinct from cyclic adenosine monophosphate dependent protein kinase and phosphorylase kinase. It is closely associated with the protein glycogen complex, but is readily separable from glycogen synthetase itself. The results suggest a promising procedure for the isolation of glycogen synthetase kinase 2 and hence the elucidation of its metabolic role.

    Original languageEnglish
    Pages (from-to)85-86
    Number of pages2
    JournalBiochemical Society Transactions
    Volume3
    Issue number1
    DOIs
    Publication statusPublished - 1 Feb 1975

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    Adenosine Kinase
    Glycogen Synthase
    Protein Kinases
    Muscle
    Skeletal Muscle
    Phosphotransferases
    Phosvitin
    Phosphorylase Kinase
    Rabbits
    Cyclic AMP-Dependent Protein Kinases
    Glycogen
    Proteins
    Cyclic AMP

    Cite this

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    title = "Glycogen synthetase kinase 2 and adenosine 3': 5' cyclic monophosphate independent protein kinase activities in rabbit skeletal muscle",
    abstract = "The major phosvitin kinase activity in skeletal muscle is distinct from cyclic adenosine monophosphate dependent protein kinase and phosphorylase kinase. It is closely associated with the protein glycogen complex, but is readily separable from glycogen synthetase itself. The results suggest a promising procedure for the isolation of glycogen synthetase kinase 2 and hence the elucidation of its metabolic role.",
    author = "Nimmo, {H. G.} and P. Cohen",
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    T1 - Glycogen synthetase kinase 2 and adenosine 3'

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    AU - Nimmo, H. G.

    AU - Cohen, P.

    PY - 1975/2/1

    Y1 - 1975/2/1

    N2 - The major phosvitin kinase activity in skeletal muscle is distinct from cyclic adenosine monophosphate dependent protein kinase and phosphorylase kinase. It is closely associated with the protein glycogen complex, but is readily separable from glycogen synthetase itself. The results suggest a promising procedure for the isolation of glycogen synthetase kinase 2 and hence the elucidation of its metabolic role.

    AB - The major phosvitin kinase activity in skeletal muscle is distinct from cyclic adenosine monophosphate dependent protein kinase and phosphorylase kinase. It is closely associated with the protein glycogen complex, but is readily separable from glycogen synthetase itself. The results suggest a promising procedure for the isolation of glycogen synthetase kinase 2 and hence the elucidation of its metabolic role.

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    JO - Biochemical Society Transactions

    JF - Biochemical Society Transactions

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