Purified lens junctional protein forms channels in planar lipid films.
Purified lens junctional protein forms channels in planar lipid films.
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纯化的晶状体连接蛋白在平面脂质膜中形成通道。
DOI：
10.1073/pnas.82.24.8468
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发表时间：
1985
影响因子：
11.1
通讯作者：
Kreman,M
中科院分区：
文献类型：
--
作者：
Zampighi,GA;Hall,JE;Kreman,M
从牛晶状体中分离的连接点用辛烷基葡萄糖苷溶解，它们的蛋白质在单层小泡中重组。在囊泡破裂面上，蛋白质以直径约为10nm的环状膜内颗粒的形式出现。在预先形成的脂质膜两侧加入含有囊泡的连接蛋白可诱导电压依赖性通道。通道在0.1 M盐溶液中具有200 pS的电导，因此足够大，可以解释完整透镜纤维之间观察到的电耦合；当电压的大小增加和辛醇存在时，它们会关闭。虽然重组通道作为晶状体纤维之间的通讯途径的身份仍有待证实，但重组通道最有可能是由MIP-26形成的，MIP-26是孤立晶状体连接的主要蛋白质成分。
Junctions isolated from bovine lenses were solubilized with the detergent octyl glucoside, and their protein(s) was reconstituted in unilamellar vesicles. The protein(s) appears as annular-shaped intramembrane particles approximately equal to 10 nm in diameter on the vesicles' fracture faces. The addition of the vesicle-containing junctional protein(s) to both sides of preformed lipid films induced voltage-dependent channels. The channels have a conductance of 200 pS in 0.1 M salt solutions and are thus large enough to account for the electrical coupling observed between intact lens fibers; they turn off when the magnitude of the voltage is increased and in the presence of octanol. Although the identity of the reconstituted channels as the communicating pathway between lens fibers remains to be proven, it is most likely that the reconstituted channels are formed by MIP-26, the major protein component of the isolated lens junctions.