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Updated: Aug 18, 2026

In Vitro Polymerization of F-actin on Early Endosomes
Published on: August 28, 2017
Product release is not the rate-limiting step during cytochalasin B-induced ATPase activity of monomeric actin
1Institut für Zoologie, Technischen Hochschule, Bundesrepublik Deutschland.
Abstract:
Under conditions where cytochalasin B induces ATPase activity of monomeric actin (0.3 mM MgCl2, 1 mM EGTA, 30 microns cytochalasin B, 1 mM ATP) the rate constant of the exchange of actin-bound epsilon-ATP for free ATP is about 4-6 times faster than steady state ATPase activity. When a stoichiometric ATP-actin complex is extracted with PCA (single turnover experiment) the apparent rate constant of Pi generation is not faster than steady state ATPase activity. - The experiments suggest that the hydrolysis of actin-bound ATP and not the subsequent release of hydrolysis products is rate-limiting during cytochalasin-induced ATPase activity of actin.
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