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微粒体的无细胞系统中一起翻译了两种大鼠去唾液酸糖蛋白受体多肽的RNA,并使用区分这两种蛋白的抗体对产品进行了免疫沉淀。在该系统中,蛋白质通过与任何亚基特异性抗血清共沉淀来寡聚。在没有微粒体的情况下合成的亚基之间或在去污剂溶解过程中混合的单独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。我们计算出低聚进行的效率约为85%。受体复合物似乎代表特定的寡聚物,因为它排除了在同一反应中合成的第三膜糖蛋白。脱唾液酸糖蛋白受体的体外低聚应该提供一个有用的系统来研究膜-蛋白复合物的组装。

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