Myosin light chain phosphorylation and phosphorylase a activity in rat extensor digitorum longus muscle

David R. Manning, James T. Stull

Research output: Contribution to journalArticle

95 Scopus citations

Abstract

Phosphorylation of the 18,500 dalton light chain of myosin and conversion of phosphorylase b to a were examined in relation to isometric tension development. Following a l sec tetanic contraction, light chain phosphate content increased from a pre-tetanic value of 0.10 to 0.75 mol phosphate/mol at 7 sec; phosphorylase a activity (ratio of activity -5′AMP +5′AMP) increased from 0.03 to 0.42 at 4 sec and decreased to control values within 20 sec. Light chain phosphate content, however, declined much more slowly and correlated to post-tetanic potentiation of peak twitch tension. Our results suggest light chain phosphorylation is not obligatory for contraction but may play a role in post-tetanic potentiation.

Original languageEnglish (US)
Pages (from-to)164-170
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume90
Issue number1
DOIs
StatePublished - Sep 12 1979

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ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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