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Effect of cytochalasin B on formation and properties of muscle F-actin

MPG-Autoren
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Löw,  Irmentraut
Max Planck Institute for Medical Research, Max Planck Society;

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Dancker,  Peter
Max Planck Institute for Medical Research, Max Planck Society;

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Zitation

Löw, I., & Dancker, P. (1976). Effect of cytochalasin B on formation and properties of muscle F-actin. Biochimica et Biophysica Acta: BBA, 430(2), 366-374. doi:10.1016/0005-2728(76)90092-X.


Zitierlink: http://hdl.handle.net/21.11116/0000-0000-2BC2-5
Zusammenfassung
Cytochalasin B stimulated polymerization and decreased the concentration of G-actin remaining in equilibrium with F-actin filaments. Polymerization in the presence of cytochalasin B gave rise to a smaller increase of viscosity but to the same increase in light scattering, compared to polymerization in the absence of cytochalasin B. Cytochalasin B reduced the viscosity of F-actin and caused the appearance of ATP hydrolysis by F-actin. The cytochalasin B-induced ATPase activity was inhibited by concentrations of KCl higher than 50 mM. The cytochalasin B-induced ATPase activity was enhanced by ethyleneglycol bis(α-aminoethyl ether)-N,N′-tetraacetic acid and reduced by MgCl2 at concentrations higher than 0.75 mM. The findings suggest that the stability of actin filaments is reduced by cytochalasin B.