Abstract
1. The CNBr digest of troponin C from rabbit fast skeletal muscle was shown to possess many of the functional properties of the whole troponin C molecule. 2. A peptide corresponding to residues 83-134 was isolated, which forms a Ca(2+-dependent complex with troponin I and neutralizes the inhibition by troponin I of the Mg(2+-stimulated adenosine triphosphatase of desensitized actomyosin. 3. The peptide inhibits the phosphorylation of fast-skeletal-muscle, but not cardiac-muscle, troponin I, by 3' :5'-cyclic AMP-dependent protein kinase. In this property it was as effective as whole skeletal-muscle troponin C when compared on a molar basis. 4. Biological activity was also present in other fractions obtained from the CNBr digest. 5. By gel filtration and affinity chromatography of the whole CNBr digest of troponin C, two peptides, one of which was identified as representing residues 83-134, were shown to form Ca(2+-dependent complexes with troponin I. 6. The significance of these findings for the mechanism of interaction of troponin C and troponin I is discussed.
MeSH Terms
Adenosine Triphosphatases/antagonists & inhibitors
Amino Acids/analysis
Calcium/metabolism
Chromatography, Affinity
Chromatography, Gel
Cyanogen Bromide
Electrophoresis, Polyacrylamide Gel
Muscle Proteins/metabolism
Peptide Fragments/isolation & purification,pharmacology
Protein Kinase Inhibitors
Troponin/metabolism
Chemicals
Amino Acids
Muscle Proteins
Peptide Fragments
Protein Kinase Inhibitors
Troponin
Adenosine Triphosphatases
Cyanogen Bromide
Calcium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Weeks R A
Perry S V
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29 references, click to expand
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