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PMID: 3158745 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Removal of tropomyosin overlap and the co-operative response to increasing calcium concentrations of the acto-subfragment-1 ATPase.

Journal of molecular biology ·Vol. 182 ·No. 2 ·1985-03-20 ·Pages 265-9

Walsh TP, Trueblood CE, Evans R, Weber A

Abstract

The co-operative response of regulated actomyosin ATPase to increasing concentrations of calcium has been attributed to nearest-neighbor interactions, presumably between troponin-tropomyosin complexes. The degree of co-operativity was not decreased after the carboxy-terminal 11 amino acid residues had been removed from tropomyosin by carboxypeptidase A. This indicates that the interactions between neighboring troponin-tropomyosin complexes do not occur through the overlapping tropomyosin ends.

MeSH Terms
Actins/metabolism Adenosine Triphosphatases/metabolism Adenosine Triphosphate/metabolism Allosteric Regulation Animals Calcium Muscles/analysis Myosin Subfragments Myosins/metabolism Peptide Fragments/metabolism Rabbits Tropomyosin/metabolism Troponin/metabolism
Chemicals
Actins Myosin Subfragments Peptide Fragments Tropomyosin Troponin Adenosine Triphosphate Adenosine Triphosphatases Myosins Calcium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Walsh T P
Trueblood C E
Evans R
Weber A
Article Info
Journal
Journal of molecular biology
Abbr.
J Mol Biol
ISSN
0022-2836
Published
1985-03-20
Pages
265-9
Language
English
Region
England
NLM ID
2985088R
Subset
IM
Grants
NHLBI NIH HHS · HL15692 · United States
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