TY - JOUR
T1 - Phosphorylation of liver pyruvate kinase by Ca++ /calmodulin-dependent protein kinase
T2 - Characterization of two phosphorylation sites
AU - Soderling, Thomas R.
AU - Schworer, Charles M.
AU - Raafat El-Maghrabi, M.
AU - Pilkis, Simon J.
N1 - Funding Information:
* Supported in part by National Institutes of Health Grant AM 17808 (TRS). + Current Address: Department of Physiology and Biophysics, State University of New York, Stony Brook, NY 11794-8661. Abbreviations used: CaM, calmodulin; HPLC, high performance liquid chromatography.
PY - 1986/9/30
Y1 - 1986/9/30
N2 - 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.
AB - 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.
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U2 - 10.1016/S0006-291X(86)80279-0
DO - 10.1016/S0006-291X(86)80279-0
M3 - Article
C2 - 3094523
AN - SCOPUS:0023037086
SN - 0006-291X
VL - 139
SP - 1017
EP - 1023
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -