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

doi:10.1016/S0006-291X(86)80279-0

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 journal › Article › peer-review

15 Scopus citations

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 language	English (US)
Pages (from-to)	1017-1023
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	139
Issue number	3
DOIs	https://doi.org/10.1016/S0006-291X(86)80279-0
State	Published - Sep 30 1986
Externally published	Yes

Funding

* 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.

Funders	Funder number
Author National Institutes of Health National Institutes of Health National Institutes of Health National Institutes of Health The Bev Hartig Huntington's Disease Foundation National Institutes of Health	AM 17808

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1016/S0006-291X(86)80279-0

Cite this

Phosphorylation of liver pyruvate kinase by Ca⁺⁺ /calmodulin-dependent protein kinase: Characterization of two phosphorylation sites. / Soderling, Thomas R.; Schworer, Charles M.; Raafat El-Maghrabi, M. et al.
In: Biochemical and Biophysical Research Communications, Vol. 139, No. 3, 30.09.1986, p. 1017-1023.

Research output: Contribution to journal › Article › peer-review

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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.",

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note = "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.",

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AU - Pilkis, Simon J.

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