Novel method for evaluation of the oligomeric structure of membrane proteins
Novel method for evaluation of the oligomeric structure of membrane proteins
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DOI：
10.1042/0264-6021:3420119
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发表时间：
1999-08-15
影响因子：
4.1
通讯作者：
Bear, CE
中科院分区：
文献类型：
--
作者：
Ramjeesingh, M;Huan, LJ;Bear, CE
通过 PAGE 评估膜蛋白的四级结构一直存在问题，因为它们在非解离去污剂中的溶解度相对较差。在这里，我们报告使用全氟辛酸（PFO）去垢剂可以很容易地将几种膜蛋白溶解在其天然四级结构中。此外，PFO 可以与 PAGE 结合使用，从而提供一种新颖且易于使用的工具，用于评估同源多聚体蛋白质复合物的分子量。
Assessment of the quaternary structure of membrane proteins by PAGE has been problematic owing to their relatively poor solubility in non-dissociative detergents. Here we report that several membrane proteins can be readily solubilized in their native quaternary structure with the use of the detergent perfluoro-octanoic acid (PFO). Further, PFO can be used with PAGE, thereby providing a novel, accessible tool with which to assess the molecular mass of homo-multimeric protein complexes.