Phosphorylation of liver pyruvate kinase by Ca++ /calmodulin-dependent protein kinase

Characterization of two phosphorylation sites

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

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

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
Volume139
Issue number3
DOIs
StatePublished - Sep 30 1986
Externally publishedYes

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Calcium-Calmodulin-Dependent Protein Kinases
Phosphorylation
Pyruvate Kinase
Liver
Thermolysin
Threonine
Protein Kinases
Serine
Sequence Analysis
Rats
High Pressure Liquid Chromatography
Calcium

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Phosphorylation of liver pyruvate kinase by Ca++ /calmodulin-dependent protein kinase : Characterization of two phosphorylation sites. / Soderling, Thomas; Schworer, Charles M.; Raafat El-Maghrabi, M.; Pilkis, Simon J.

In: Biochemical and Biophysical Research Communications, Vol. 139, No. 3, 30.09.1986, p. 1017-1023.

Research output: Contribution to journalArticle

Soderling, Thomas ; Schworer, Charles M. ; Raafat El-Maghrabi, M. ; Pilkis, Simon J. / Phosphorylation of liver pyruvate kinase by Ca++ /calmodulin-dependent protein kinase : Characterization of two phosphorylation sites. In: Biochemical and Biophysical Research Communications. 1986 ; Vol. 139, No. 3. pp. 1017-1023.
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