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 language | English (US) |
---|---|
Pages (from-to) | 334-336 |
Number of pages | 3 |
Journal | Journal of Biological Chemistry |
Volume | 253 |
Issue number | 2 |
State | Published - 1978 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology