PMID: 3754154Feb 11, 1986Paper

Calmodulin-linked equilibria in smooth muscle myosin light chain kinase

Biochemistry
D A Malencik, S R Anderson

Abstract

Competition experiments using 9-anthroylcholine, a fluorescent dye that undergoes calmodulin-dependent binding by smooth muscle myosin light chain kinase [Malencik, D. A., Anderson, S. R., Bohnert, J. L., & Shalitin, Y. S. (1982) Biochemistry 21, 4031], demonstrate a strongly stabilizing interaction between the adenosine 5'-triphosphate and myosin light chain binding sites operating within the enzyme-calmodulin complex but probably not in the free enzyme. The interactions in the latter case may be even slightly destabilizing. The fluorescence enhancement in solutions containing 5.0 microM each of the enzyme and calmodulin is directly proportional to the maximum possible concentration of bound calcium on the basis of four calcium binding sites. Evidently, all four calcium binding sites of calmodulin contribute about equally to the enhanced binding of 9-anthroylcholine by the enzyme. Fluorescence titrations on solutions containing 1.0 microM enzyme plus calmodulin yield a Hill coefficient of 1.2 and K = 0.35 +/- 0.08 microM calcium. Three proteolytic fragments of smooth muscle myosin light chain kinase, apparent products of endogenous proteolysis, were isolated and characterized. All three possess calmodulin-dependent catalytic a...Continue Reading

Citations

Nov 1, 1989·Archives of Biochemistry and Biophysics·C J Yuan, D J Graves
Sep 1, 1995·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·J V Small
Feb 10, 1987·Biochemistry·D A Malencik, S R Anderson
Feb 9, 1988·Biochemistry·D A Malencik, S R Anderson
Mar 22, 1988·Biochemistry·D A Malencik, S R Anderson
Apr 1, 1990·Journal of Muscle Research and Cell Motility·A Sobieszek
Nov 15, 1994·Biochemistry·D A Malencik, S R Anderson

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