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Science 10 June 1983:
Vol. 220. no. 4602, pp. 1167 - 1169
DOI: 10.1126/science.6857239
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Articles

Science, Vol 220, Issue 4602, 1167-1169
Copyright © 1983 by American Association for the Advancement of Science

articles

Myosin light chain phosphorylation does not modulate cross-bridge cycling rate in mouse skeletal muscle

TM Butler, MJ Siegman, SU Mooers, and RJ Barsotti

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.


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