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PMID: 1454820 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Effect of Ca2+ on weak cross-bridge interaction with actin in the presence of adenosine 5'-[gamma-thio]triphosphate).

Kraft T, Yu LC, Kuhn HJ, Brenner B

Abstract

In the presence of the nucleotide analog adenosine 5'-[gamma-thio]triphosphate (ATP[gamma S]), effects of Ca2+ on stiffness and equatorial x-ray diffraction patterns of single skinned fibers of the rabbit psoas muscle were studied. It is shown that cross-bridges in the presence of ATP[gamma S] have properties of the weak-binding states of the ATP hydrolysis cycle. Raising the Ca2+ concentration up to pCa 4.5 has little effect on actin affinity of cross-bridges in the presence of ATP[gamma S]. However, the rate constants for cross-bridge dissociation and reassociation from and to actin are reduced by about 2 orders of magnitude. In addition, nucleotide affinity of the cross-bridge is much smaller at high Ca2+ concentrations. Implications for interpretation of fiber stiffness recorded during isotonic shortening and the rising phase of a tetanus are discussed.

MeSH Terms
Actins/metabolism Actomyosin/physiology Adenosine Triphosphate/analogs & derivatives,metabolism Animals Calcium/physiology In Vitro Techniques Kinetics Motion Muscle Contraction Protein Binding Rabbits
Chemicals
Actins adenosine 5'-O-(3-thiotriphosphate) Adenosine Triphosphate Actomyosin Calcium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Kraft T
Department of General Physiology, University of Ulm, Federal Republic of Germany.
Yu L C
Kuhn H J
Brenner B
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37 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1992-12-01
Pages
11362-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC50550
Subset
IM
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