Dunia I, Manenti S, Rousselet A, Benedetti E L
Institut Jacques Monod--Centre National de la Recherche Scientifique CNRS, Université Paris VII, France.
J Cell Biol. 1987 Oct;105(4):1679-89. doi: 10.1083/jcb.105.4.1679.
The purified major intrinsic protein of the lens fiber plasma membrane (MP26) reconstituted into liposomes favored membrane-to-membrane close contacts as visualized by freeze fracture and immunoelectron microscopy. Reconstituted apposed unilamellar vesicles formed pentalaminar profiles, and multilamellar liposomes showed regions of stacked bilayers. Immunogold labeling, using antibody directed against MP26, demonstrated that this polypeptide is present in regions of membrane-to-membrane close interaction. Fracture faces displayed both randomly distributed clusters of 8-nm polygonal intramembrane particles and membrane domains where a bidimensional lattice of repeating subunits was present. The structural pleomorphism which characterized the MP26-reconstituted proteoliposomes seems quite comparable to that visualized in natural fiber plasma membrane domains.
纯化的晶状体纤维质膜主要内在蛋白（MP26）重构到脂质体中，通过冷冻断裂和免疫电子显微镜观察发现，其有利于膜与膜之间的紧密接触。重构的并列单层囊泡形成了五片层结构，多层脂质体显示出双层堆叠区域。使用针对MP26的抗体进行免疫金标记表明，该多肽存在于膜与膜紧密相互作用的区域。断裂面既显示出8纳米多边形膜内颗粒的随机分布簇，也显示出存在重复亚基二维晶格的膜结构域。表征MP26重构蛋白脂质体的结构多态性似乎与天然纤维质膜结构域中观察到的结构多态性相当。
