We have translated RNAs for the two rat asialoglycoprotein receptor polypeptides together in a cell-free system containing dog pancreatic microsomes and immunoprecipitated the products with antibodies that distinguish the two proteins. In this system the proteins oligomerize, as judged by their coprecipitation with either of the subunit-specific antisera. Oligomerization does not occur between subunits synthesized without microsomes or between subunits synthesized on separate microsomes mixed during detergent solubilization. Thus, oligomerization occurs within the microsomal membrane. We calculate that oligomerization proceeds with an efficiency of approximately 85%. The receptor complex appears to represent a specific oligomer because it excludes a third membrane glycoprotein synthesized in the same reaction. Oligomerization of the asialoglycoprotein receptor in vitro should provide a useful system to study the assembly of a membrane-protein complex.

译文

我们已经在包含狗胰腺微粒体的无细胞系统中将两种大鼠去唾液酸糖蛋白受体多肽的rna翻译在一起,并用区分这两种蛋白质的抗体免疫沉淀了产物。在该系统中,蛋白质寡聚,根据它们与亚基特异性抗血清中的任何一种的共沉淀来判断。在没有微粒体的情况下合成的亚基之间或在洗涤剂增溶过程中混合的单独的微粒体上合成的亚基之间不会发生低聚。因此,低聚发生在微粒体膜内。我们计算低聚化以约85% 的效率进行。受体复合物似乎代表特定的寡聚体,因为它排除了在同一反应中合成的第三种膜糖蛋白。体外去唾液酸糖蛋白受体的寡聚化应为研究膜蛋白复合物的组装提供有用的系统。

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