Caron J M, Berlin R D
J Cell Biol. 1979 Jun;81(3):665-71. doi: 10.1083/jcb.81.3.665.
We have examined the interaction of unilamellar dimyristoyl phosphatidylcholine liposomes with the high-speed supernate of brain homogenate and with tubulin purified through one or two cycles of microtubule assembly-disassembly. Tubulin and certian high molecular weight proteins are selectively adsorbed from these mixtures onto liposomes. The composition of adsorbed proteins is similar to that obtained during corresponding cycles of microtubule assembly, suggesting the equivalency of these processes. Adsorption induces stacking and/or fusion of liposomes into multilamellar structures indicating strong protein-lipid interaction. In addition, liposome-adsorbed tubulin forms extensive intermolecular disulfide bridges that are inert to reducing agents in the aqueous medium. The observations form a basis for further study of the distribution, function, and properties of membrane-bound tubulin.
我们研究了单层二肉豆蔻酰磷脂酰胆碱脂质体与脑匀浆高速上清液以及通过一两个微管组装-拆卸循环纯化的微管蛋白之间的相互作用。微管蛋白和某些高分子量蛋白质从这些混合物中选择性地吸附到脂质体上。吸附蛋白质的组成与在微管组装的相应循环中获得的组成相似,表明这些过程是等效的。吸附诱导脂质体堆叠和/或融合成多层结构,表明蛋白质-脂质之间有强烈的相互作用。此外,脂质体吸附的微管蛋白形成广泛的分子间二硫键,这些二硫键在水性介质中对还原剂呈惰性。这些观察结果为进一步研究膜结合微管蛋白的分布、功能和特性奠定了基础。