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JBC, Vol. 253, Issue 23, 8347-8350, Dec, 1978
R. S. Adelstein, M. A. Conti, D. R. Hathaway and C. B. Klee
Turkey gizzard smooth muscle light chain kinase was purified by affinity
chromatography on calcium dependent regulator weight of 125,000 +/- 5,000
in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. When myosin
light chain kinase is incubated with the catalytic subunit of cyclic
AMP-dependent protein kinase, 1 mol of phosphate is incorporated per mol of
myosin kinase. Brief tryptic digestion of the 32P-labeled myosin kinase
liberates a single radioactive peptide with a molecular weight of
approximately 22,000. Phosphorylation of myosin kinase results in a 2-fold
decrease in the rate at which the enzyme phosphorylates the 20,000-dalton
light chain of smooth muscle myosin. These results suggest that cyclic AMP
has a direct effect on actin-myosin interaction in smooth muscle.
Phosphorylation of smooth muscle myosin light chain kinase by the catalytic subunit of adenosine 3': 5'-monophosphate-dependent protein kinase
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