Kinetics of Binding of Caldesmon to Actin
Chalovich, Joseph M.; Chen, Yi-Der; Dudek, Ronald; 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-l,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 107 M-1 s-1 and 18.2 s-1, 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 -1. 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-l,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. Originally published in the Journal of Biological Chemistry, Vol. 270, No. 17, 1995.
Chalovich, Joseph M., & Chen, Yi-Der, & Dudek, Ronald, & Hai, Luo. (April 1995). Kinetics of Binding of Caldesmon to Actin. Journal of Biological Chemistry, 270(17), 9911- 9916. Retrieved from http://hdl.handle.net/10342/2994
Chalovich, Joseph M., and Chen, Yi-Der, and Dudek, Ronald, and Hai, Luo. "Kinetics of Binding of Caldesmon to Actin". Journal of Biological Chemistry. 270:17. (9911-9916), April 1995. August 17, 2018. http://hdl.handle.net/10342/2994.
Chalovich, Joseph M. and Chen, Yi-Der and Dudek, Ronald and Hai, Luo, "Kinetics of Binding of Caldesmon to Actin," Journal of Biological Chemistry 270, no. 17 (April 1995), http://hdl.handle.net/10342/2994 (accessed August 17, 2018).
Chalovich, Joseph M., Chen, Yi-Der, Dudek, Ronald, Hai, Luo. Kinetics of Binding of Caldesmon to Actin. Journal of Biological Chemistry. April 1995; 270(17): 9911-9916. http://hdl.handle.net/10342/2994. Accessed August 17, 2018.
East Carolina University