Molecular characterization of rat skeletal muscle myosin light chain kinase

B. P. Herring, M. H. Nunnally, P. J. Gallagher, J. T. Stull

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

A 1.85-kilobase (kb) cDNA has been isolated that encodes the catalytic and calmodulin binding domains of rat skeletal muscle myosin light chain kinase. The cDNA hybridized to a 3.3-kb RNA present in fast- and slow-twitch skeletal muscles. The reported enzymatic activity (3-fold greater in fast- than slow-twitch skeletal muscles) reflects the relative abundance of this RNA in the two types of skeletal muscle. No hybridization of the cDNA was detected to RNA isolated from smooth or nonmuscle tissues. The clone cross hybridized to a 2.2-kb RNA present in cardiac tissue. Ribonuclease protection analysis of skeletal and cardiac muscle RNA revealed major differences in the two hybridizing RNAs. Thus rats skeletal muscle contains a single myosin light chain kinase isoform, which is distinct from the cardiac, smooth, and nonmuscle forms.

Original languageEnglish (US)
Pages (from-to)25/2
JournalAmerican Journal of Physiology - Cell Physiology
Volume256
Issue number2
StatePublished - Jan 1 1989

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

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    Herring, B. P., Nunnally, M. H., Gallagher, P. J., & Stull, J. T. (1989). Molecular characterization of rat skeletal muscle myosin light chain kinase. American Journal of Physiology - Cell Physiology, 256(2), 25/2.