Coué M, Brenner S L, Spector I, Korn E D
FEBS Lett. 1987 Mar 23;213(2):316-8. doi: 10.1016/0014-5793(87)81513-2.
Latrunculin A, a toxin purified from the red sea sponge Latrunculia magnifica, was found previously to induce striking reversible changes in the morphology of mammalian cells in culture and to disrupt the organization of their microfilaments. We now provide evidence that latrunculin A affects the polymerization of pure actin in vitro in a manner consistent with the formation of a 1:1 molar complex between latrunculin A and G-actin. The equilibrium dissociation constant (Kd) for the reaction in vitro is about 0.2 microM whereas the effects of the drug on cultured cells are detectable at concentrations in the medium of 0.1-1 microM.
拉特runculin A是一种从红海海绵巨大拉特runculia中纯化得到的毒素，先前发现它能在培养的哺乳动物细胞形态上诱导显著的可逆变化，并破坏其微丝的组织。我们现在提供证据表明，拉特runculin A以一种与拉特runculin A和G-肌动蛋白之间形成1:1摩尔复合物相一致的方式影响体外纯肌动蛋白的聚合。体外反应的平衡解离常数（Kd）约为0.2微摩尔，而该药物在培养基中浓度为0.1 - 1微摩尔时对培养细胞的影响即可检测到。
