PMID: 1212218Oct 1, 1975Paper

Phosphorylation of the light-chain components of myosin from cardiac and red skeletal muscles

The Biochemical Journal
N Frearson, S V Perry

Abstract

1. The light-chain components of myosin from cardiac muscle (19000 and 27000 daltons) and of rabbit soleus and crureus muscles (19000, 27000 and 29000 daltons) were characterized. 2. The 19000-dalton components in carciac- and red-skeletal-muscle myosins were spontaneously modified to a component of slightly higher net negative charge. 3. The 19000-dalton component in cardiac and red skeletal muscles and their modified forms were phosphorylated by myosin light-chain kinase. 4. Evidence was obtained for the presence of myosin light-chain kinase in cardiac and red skeletal muscles. 5. Myosin light-chain kinase catalysed the phosphorylation of the whole light-chain fraction from white and red skeletal muscle at similar rates. The light-chain fraction of cardiac-muscle myosin was phosphorylated at a significantly lower rate. 6. The light-chain components of cardiac-muscle myosin and their phosphorylated froms were separated by ion-exchange chromatography and their amino acid compositions determined.

Citations

Jan 26, 2016·Biochemical and Biophysical Research Communications·Hilde EikemoJan-Bjørn Osnes
Aug 24, 2013·Trends in Cardiovascular Medicine·Farah SheikhJu Chen
Nov 1, 1977·European Journal of Biochemistry·F LamyJ E Dumont
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