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

50 Scopus citations

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 K(m) values for troponin, but the V(max) 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)334-336
Number of pages3
JournalJournal of Biological Chemistry
Volume253
Issue number2
StatePublished - Jan 1 1978

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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