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PMID: 145626 Published · ppublish English Journal Article

Phosphorylation of cardiac myofibrillar proteins.

Recent advances in studies on cardiac structure and metabolism ·Vol. 11 ·1976-00-00 ·Pages 111-20

Cole HA, Frearson N, Moir AJ, Perry SV, Solaro RJ

Abstract

The P light chain of cardiac myosin is phosphorylated and dephosphorylated by highly specific enzymes. These reactions take place in the beating rabbit heart and there is evidence that dephosphorylation of the light chain occurs during the inotropic response produced by adrenaline. The extent of phosphorylation of cardiac troponin I is determined by the functional state of the beating heart. During perfusion of the rabbit heart the basal phosphate content of troponin I increased from the basal level of about 1.5 moles P per mole to about 2.7 moles P per mole at the height of the inotropic response to adrenaline. The three sites of phosphorylation on troponin I are probably located in the N terminal cyanogen bromide peptide of 48 residues.

MeSH Terms
Adenosine Triphosphatases/metabolism Animals Calcium/pharmacology Kinetics Macromolecular Substances Molecular Weight Myocardial Contraction Myocardium/metabolism Myosins/metabolism Perfusion Phosphoproteins/metabolism Protein Kinases/metabolism Rabbits Troponin/metabolism
Chemicals
Macromolecular Substances Phosphoproteins Troponin Protein Kinases Adenosine Triphosphatases Myosins Calcium
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Cole H A
Frearson N
Moir A J
Perry S V
Solaro R J
Article Info
Journal
Recent advances in studies on cardiac structure and metabolism
Abbr.
Recent Adv Stud Cardiac Struct Metab
ISSN
0363-5872
Published
1976-00-00
Pages
111-20
Language
English
Region
United States
NLM ID
0325677
Subset
IM
External Links
PubMed source
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