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PMID: 6455170 Published · ppublish English Journal Article

Theoretical models for cooperative steady-state ATPase activity of myosin subfragment-1 on regulated actin.

Biophysical journal ·Vol. 35 ·No. 1 ·1981-07-00 ·Pages 99-112

Hill TL, Eisenberg E, Chalovich JM

Abstract

Recent theoretical work on the cooperative equilibrium binding of myosin subfragment-1-ADP to regulated actin, as influenced by Ca2+, is extended here to the cooperative steady-state ATPase activity of myosin subfragment-1 on regulated actin. Exact solution of the general steady-state problem will require Monte Carlo calculations. Three interrelated special cases are discussed in some detail and sample computer (not Monte Carlo) solutions are given. The eventual objective is to apply these considerations to in vitro experimental data and to in vivo muscle models.

MeSH Terms
Actins/pharmacology Adenosine Triphosphatases/metabolism Homeostasis Models, Biological Myosin Subfragments Myosins/analysis,pharmacology Peptide Fragments/pharmacology
Chemicals
Actins Myosin Subfragments Peptide Fragments Adenosine Triphosphatases Myosins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Hill T L
Eisenberg E
Chalovich J M
References (18)
18 references, click to expand
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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
Published
1981-07-00
Pages
99-112
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1327506
Subset
IM
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