Insight into the kinetics and the mode of the interaction between smooth muscle calponin and F-actin.

Janusz Kołakowski; Renata Dabrowska

doi:10.18388/abp.2002_3806

Insight into the kinetics and the mode of the interaction between smooth muscle calponin and F-actin.

Janusz Kołakowski Department of Muscle Biochemistry, Nencki Institute of Experimental Biology, Warszawa, Poland.;
Renata Dabrowska

DOI: https://doi.org/10.18388/abp.2002_3806

Abstract

Kinetics of the smooth muscle calponin-F-actin interaction was studied by stopped-flow measurements of light scattering and fluorescence intensity of pyrene-labelled F-actin. The intensity and character of the changes in light scattering, and thus the mode of calponin binding to actin filaments leading to changes in their shape and bundling, depend on the molar ratio of the two proteins. Parallel measurements of pyrene-fluorescence quenching upon calponin binding revealed that intrinsic conformational changes in actin filaments are delayed relative to the binding process and are not markedly influenced by the mode of calponin binding. Bundling of actin filaments by calponin was not correlated with fluorescence changes and thus with alterations in the structure of actin filaments.

Published

2002-06-30

Issue

Vol. 49 No. 2 (2002)

Section

Articles

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