Effect of cytochalasin B on formation and properties of muscle F-actin |
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Authors: | I. Löw P. Dancker |
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Affiliation: | 1. Max-Planck-Institut für medizinische Forschung, Abteilung Naturstoff-Chemie Heidelberg, Jahnstr. 29 G.F.R.;2. Abteilung Physiologie D-69 Heidelberg, Jahnstr. 29 G.F.R. |
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Abstract: | 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. |
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Keywords: | EGTA |
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