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Volume 270, Number 17, Issue of April 28, pp. 9911-9916, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Kinetics of Binding of Caldesmon to Actin

Joseph M. Chalovich , Yi-der Chen , Ronald Dudek , Hai Luo

The time course of interaction of caldesmon with actin may be monitored by fluorescence changes that occur upon the binding of 12-( N-methyl- N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl))-labeled caldesmon to actin or to acrylodan actin. The concentration dependence of the observed rate of caldesmon-actin binding was analyzed to a first approximation as a single-step reaction using a Monte Carlo simulation. The derived association and dissociation rates were 10 Msand 18.2 s, respectively. Smooth muscle tropomyosin enhances the binding of caldesmon to actin, and this was found to be due to a reduction in the rate of dissociation to 6.3 s. There is no evidence from this study for a different mechanism of binding in the presence of tropomyosin. The fluorescence changes that occurred with the binding of 12-( N - methyl - N - (7 - nitrobenz-2-oxa-1,3-diazol-4-yl))-labeled caldesmon to actin or actin-tropomyosin were reversed by the addition of myosin subfragment 1 as predicted by a competitive binding mechanism.



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Y. Yamakita, F. Oosawa, S. Yamashiro, and F. Matsumura
Caldesmon Inhibits Arp2/3-mediated Actin Nucleation
J. Biol. Chem., May 9, 2003; 278(20): 17937 - 17944.
[Abstract] [Full Text] [PDF]


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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.