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PMID: 2524187 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

A tight-binding interaction between smooth-muscle native thin filaments and heavy meromyosin in the presence of MgATP.

The Biochemical journal ·Vol. 259 ·No. 1 ·1989-04-01 ·Pages 303-6

Marston SB

Abstract

The binding of the Ca2+-regulated native thin filaments from vascular smooth muscle to vascular smooth-muscle heavy meromyosin was measured in the presence of 3 mM-MgATP. At 25 degrees C and I 0.25 binding had an affinity of 1 X 10(-6)-0.3 X 10(-6) M-1 with a stoichiometry of one molecule bound to one actin monomer. The Km for the activation of heavy-meromyosin ATPase was 20-50 microM. Thin filament-heavy meromyosin binding was not altered by Ca2+ (pCa 9-4) or the extent of myosin phosphorylation. With skeletal-muscle heavy meromyosin affinity was 0.023 X 10(6) M-1 in parallel with activation of the ATPase (Km 54 microM). It is concluded that tight binding is specific to smooth-muscle proteins and that it is not related to the ATPase activation site.

MeSH Terms
Actin Cytoskeleton/metabolism Adenosine Triphosphate/metabolism Animals Ca(2+) Mg(2+)-ATPase/metabolism Calcium/metabolism Cytoskeleton/metabolism Enzyme Activation Muscle, Smooth, Vascular/metabolism Myosin Subfragments/metabolism Myosins/metabolism
Chemicals
Myosin Subfragments Adenosine Triphosphate Ca(2+) Mg(2+)-ATPase Myosins Calcium
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Marston S B
National Heart and Lung Institute, London, U.K.
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24 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2590303
Published
1989-04-01
Pages
303-6
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1138506
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2590303 PMC Full Text View journal details
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