Novel method for evaluation of the oligomeric structure of membrane proteins

被引：122

作者：

Ramjeesingh, M ^{[1
]}

Huan, LJ ^{[1
]}

Garami, E ^{[1
]}

Bear, CE ^{[1
]}

机构：

[1] Hosp Sick Children, Res Inst, Dept Cell Biol, Toronto, ON M5G 1X8, Canada

来源：

BIOCHEMICAL JOURNAL | 1999年 / 342卷

关键词：

ion channels; multimeric complexes; quaternary structure; SDS/PAGE;

D O I：

10.1042/0264-6021:3420119

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：119 / 123

页数：5

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