Complex Influence of Cytochalasin B on Actin Polymerization

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Abstract
In the presence of very low concentrations (about 2 .times. 10-7 M) of cytochalasin B (CB) the time course of [rabbit skeletal muscle] actin polymerization is much more sigmoidal when followed by viscosity measurements than when followed by light scattering measurements. Under these conditions actin polymers do not immediately reach their final length but only via short bent polymers which can be detected only by light scattering but not by viscosity measurements. At higher CB concentrations (about equimolar to those of actin) CB reduces the average degree of polymerization and favors the nucleation step necessary for polymerization.