Inhibition of actin polymerization by latrunculin A

摘要: Abstract Latrunculin A, a toxin purified from the red sea sponge Latrunculia magnifica , was found previously to induce striking reversible changes in morphology of mammalian cells culture and disrupt organization their microfilaments. We now provide evidence that latrunculin A affects polymerization pureactin vitro manner consistent with formation 1:1 molar complex between G-actin. The equilibrium dissociation constant ( K d ) for reaction is about 0.2 μM whereas effects drug on cultured are detectable at concentrations medium 0.1–1 μM.