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Article
Myosin light chain phosphorylation does not modulate cross-bridge cycling rate in mouse skeletal muscle
Science
  • T. M. Butler
  • M. J. Siegman
  • S. U. Mooers
  • Robert J. Barsotti, Philadelphia College of Osteopathic Medicine
Document Type
Article
Publication Date
1-1-1983
Disciplines
Abstract
An attempt was made to determine whether phosphorylation of the myosin light chain represents a thick filament-associated mechanism for modulating the rate of cross-bridge cycling in mouse skeletal muscle. When the degree of light chain phosphorylation was varied independently of tetanus duration, there was no correlation of phosphorylation with cross-bridge turnover rate, as measured by the shortening velocity of the muscle. It is concluded that in intact skeletal muscle phosphorylation of the myosin light chain does not in itself modulate cross-bridge cycling rate and that previously reported changes in cycling rate were due to other factors that may vary with tetanus duration.
Comments

This article was published in Science, Volume 220, Issue 4602, Pages 1167-1169.

The published version is available at http://dx.doi.org/10.1126/science.6857239 .

Copyright © 1983 AAAS.

Citation Information
T. M. Butler, M. J. Siegman, S. U. Mooers and Robert J. Barsotti. "Myosin light chain phosphorylation does not modulate cross-bridge cycling rate in mouse skeletal muscle" Science Vol. 220 Iss. 4602 (1983) p. 1167 - 1169
Available at: http://works.bepress.com/robert_barsotti/33/