Duden R, Griffiths G, Frank R, Argos P, Kreis T E
European Molecular Biology Laboratory, Heidelberg, Federal Republic of Germany.
Cell. 1991 Feb 8;64(3):649-65. doi: 10.1016/0092-8674(91)90248-w.
We have cloned and sequenced beta-COP, a peripheral 110 kd Golgi membrane protein. beta-COP shows significant homology to beta-adaptin. It is present in a membrane-bound form and in a cytosolic complex of 13-14S, with a Stokes radius of approximately 10 nm and an estimated Mr of approximately 550,000. By immunofluorescence labeling, beta-COP is associated with the structures of the Golgi complex. Immunoelectron microscopy has localized beta-COP to non-clathrin-coated vesicles and cisternae of the Golgi complex. These coated vesicles accumulate in rat liver Golgi fractions treated with GTP gamma S and strongly label for beta-COP. Our data suggest that beta-COP is a component of a coat associated with vesicles and cisternae of the Golgi complex.
我们已经克隆并测序了β - 衔接蛋白（β-COP），一种分子量为110kd的外周高尔基体膜蛋白。β - 衔接蛋白与β-适配蛋白显示出显著的同源性。它以膜结合形式存在于13 - 14S的胞质复合物中，斯托克斯半径约为10nm，估计分子量约为550,000。通过免疫荧光标记，β - 衔接蛋白与高尔基体复合物的结构相关联。免疫电子显微镜已将β - 衔接蛋白定位到高尔基体复合物的非网格蛋白包被小泡和扁平囊上。在用GTPγS处理的大鼠肝脏高尔基体组分中，这些包被小泡积累并强烈标记β - 衔接蛋白。我们的数据表明，β - 衔接蛋白是与高尔基体复合物的小泡和扁平囊相关的包被的一个组成部分。
