Phosphorylation of liver pyruvate kinase by Ca++ /calmodulin-dependent protein kinase: Characterization of two phosphorylation sites

Thomas R. Soderling, Charles M. Schworer, M. Raafat El-Maghrabi, Simon J. Pilkis

    Research output: Contribution to journalArticlepeer-review

    13 Scopus citations


    Rat liver pyruvate kinase is phosphorylated by calcium/calmodulindependent protein kinase II at serine and threonine residues in a 3-4 kDa CNBr fragment located near the amino terminus. The two sites of phosphorylation were separated by reverse-phase HPLC of a thermolysin digest. Sequence analysis established the sites of phosphorylation as follows: LeuArg-Arg-Ala-Ser(PO4)-Val-Ala-Gln-Leu-Thr(PO4)-Gln-Glu.

    Original languageEnglish (US)
    Pages (from-to)1017-1023
    Number of pages7
    JournalBiochemical and Biophysical Research Communications
    Issue number3
    StatePublished - Sep 30 1986

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology

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