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PMID: 6893044 Published · ppublish English Journal Article

Interaction of C-protein with myosin.

Journal of biochemistry ·Vol. 87 ·No. 5 ·1980-05-00 ·Pages 1413-20

Miyahara M, Noda H

Abstract

The effect of C-protein on the assembly reaction of myosin was studied by flow birefringence, electron microscopy, and ultracentrifugation. Myosin filaments were formed by dilution to a lower ionic strength. Thinner filaments of 70-110 A in diameter were formed in the presence of C-protein. When dilution was effected by moderately slow dilution (dilution time of 0.5-2 min) or by stepwise dilution, C-protein favored the formation of longer filaments. When dilution was effected by even slower dilution (dilution time above 2 min), C-protein favored the formation of shorter filaments. Longer filaments formed by slow dilution incorporated more C-protein than shorter ones formed by faster dilution. Addition of C-protein to a solution of myosin filaments caused association of the filaments into longer filaments. The elongation effect was slower and stronger for longer filaments.

MeSH Terms
Animals Birefringence Carrier Proteins Kinetics Macromolecular Substances Microscopy, Electron Muscle Proteins Muscles/analysis Myosins Osmolar Concentration Protein Binding Rabbits
Chemicals
Carrier Proteins Macromolecular Substances Muscle Proteins myosin-binding protein C Myosins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Miyahara M
Noda H
Article Info
Journal
Journal of biochemistry
Abbr.
J Biochem
ISSN
0021-924X
Published
1980-05-00
Pages
1413-20
Language
English
Region
England
NLM ID
0376600
Subset
IM
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