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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