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PMID: 140712 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Dependence of energy transduction in intact skeletal muscles on the time in tension.

Biophysical journal ·Vol. 18 ·No. 2 ·1977-05-00 ·Pages 161-72

Kawai M, Brandt P, Orentlicher M

Abstract

In intact single crayfish muscle fibers and frog semitendinosus muscles we have studied the tension response to sinusoidal length changes in the frequency range of 0.25-133 Hz. By this method we have resolved three processes in the interaction of myosin cross-bridges with actin in fully activated preparations. They are (A) a low-frequency phase advance, (B) a middle-frequency delay, and (C) a high-frequency advance. These processes can be used as probes to study the chemomechanical coupling of contractility. Process (B) represents net power output from the muscle preparation (oscillatory work). With maximal K or caffeine activation of crayfish muscle at 20 degrees C, it decreases to zero in the initial 45 s of maintained tension. Similar results were obtained with frog semitendinosus whole muscles. We interpret this decrease of (B) with time as a gradual decrease in actomyosin ATP-hydrolysis rate.

MeSH Terms
Actomyosin/metabolism Adenosine Triphosphatases/metabolism Animals Anura Astacoidea Energy Transfer In Vitro Techniques Kinetics Muscle Contraction Muscles/physiology Rana pipiens
Chemicals
Actomyosin Adenosine Triphosphatases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Kawai M
Brandt P
Orentlicher M
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29 references, click to expand
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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
DOI
10.1016/S0006-3495(77)85605-1
Published
1977-05-00
Pages
161-72
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1473282
Subset
IM
External Links
PubMed source DOI: 10.1016/S0006-3495(77)85605-1 PMC Full Text View journal details
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