Phosphorylation of cardiac troponin by guanosine 3'

5'-monophosphate-dependent protein kinase.

D. K. Blumenthal, J. T. Stull, G. N. Gill

Research output: Contribution to journalArticle

Abstract

Homogeneous cGMP-dependent protein kinase catalyzes the rapid incorporation of phosphate, specifically into the inhibitory subunit of purified cardiac troponin with a maximal incorporation of 1 mol of phosphate/mol of troponin. When troponin was incubated in the presence of both cGMP- and cAMP-dependent protein kinases, a maximal incorporation of 1 mol of phosphate/mol of troponin was observed which suggested phosphorylation of the same site by the two kinases. Both cyclic nucleotide-dependent kinases had similar Km values for troponin, but the Vmax value for the phosphorylation reaction catalyzed by cAMP-dependent protein kinase was 12-fold greater than the value obtained for cGMP-dependent protein kinase.

Original languageEnglish (US)
Pages (from-to)324-326
Number of pages3
JournalJournal of Biological Chemistry
Volume253
Issue number2
StatePublished - Jan 25 1978

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Guanosine Monophosphate
Phosphorylation
Troponin
Guanosine
Protein Kinases
Cyclic GMP-Dependent Protein Kinases
Phosphates
Cyclic AMP-Dependent Protein Kinases
Phosphotransferases
Cyclic Nucleotides

ASJC Scopus subject areas

  • Biochemistry

Cite this

Phosphorylation of cardiac troponin by guanosine 3' : 5'-monophosphate-dependent protein kinase. / Blumenthal, D. K.; Stull, J. T.; Gill, G. N.

In: Journal of Biological Chemistry, Vol. 253, No. 2, 25.01.1978, p. 324-326.

Research output: Contribution to journalArticle

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