The Influence of Caldesmon on Papain Proteolysis of Monomeric Smooth Muscle Myosin

The influence of caldesmon on papain digestion of chicken gizzard monomeric myosin in folded (10S) conformation depends on its phosphorylation. Caldesmon exposes the head/rod junction of myosin in phosphorylated form to proteolytic attack (particularly in the presence of Ca2+) and slightly screens i...

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Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 225; no. 1; pp. 195 - 202
Main Authors Kulikova, Natalia, Dabrowska, Renata
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 05.08.1996
Subjects
Animals
Calmodulin-Binding Proteins - pharmacology
Chickens
Chromatography, Affinity
Electrophoresis, Polyacrylamide Gel
Gizzard, Avian
Kinetics
Muscle, Smooth - metabolism
Myosins - metabolism
Papain - metabolism
Peptide Fragments - chemistry
Peptide Fragments - isolation & purification
Time Factors
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Summary:The influence of caldesmon on papain digestion of chicken gizzard monomeric myosin in folded (10S) conformation depends on its phosphorylation. Caldesmon exposes the head/rod junction of myosin in phosphorylated form to proteolytic attack (particularly in the presence of Ca2+) and slightly screens it in unphosphorylated form. In both folded forms RLCs are protected by caldesmon, more in unphosphorylated than in phosphorylated myosin. The results indicate that the conformations of folded unphosphorylated and phosphorylated myosin are distinct and suggest that caldesmon destabilizes the regulatory domain in folded conformation of phosphorylated myosin.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1996.1153