Optimal concentrations of N-decanoyl-N-methylglucamine and sodium dodecyl sulfate allow the extraction and analysis of membrane proteins

被引：5

作者：

Chuang, Jen-Hua ^{[1
]}

Kao, Yu-Jing ^{[1
]}

Ruderman, Neil B. ^{[2
,3
]}

Tung, Li-Chu ^{[1
]}

Lin, Yenshou ^{[1
]}

机构：

[1] Natl Taiwan Normal Univ, Dept Life Sci, Taipei 116, Taiwan

[2] Boston Univ, Diabet & Metab Res Unit, Dept Med, Sch Med, Boston, MA 02118 USA

[3] Boston Univ, Endocrinol Sect, Sch Med, Boston, MA 02118 USA

来源：

ANALYTICAL BIOCHEMISTRY | 2011年 / 418卷 / 02期

关键词：

Integral membrane proteins; Membrane proteins; SDS; MEGA-10; CMC; ADIPONECTIN RECEPTORS; FRACTIONATION; DETERGENTS; CELLS; BINDS;

D O I：

10.1016/j.ab.2011.08.006

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

We studied the extraction and analysis of integral membrane proteins possessing hydrophobic and hydrophilic domains and found that a nonionic detergent called MEGA-10, used in lysis buffers, had a superior extraction effect compared to most conventional detergents. A sodium dodecyl sulfate (SDS) concentration of >0.4% (w/v) in the sample buffer was crucial for those proteins to be clearly analyzed by electrophoresis and Western blotting. Furthermore, MEGA-10 had the tendency to maximally extract proteins around its critical micelle concentration (CMC) of 0.24% (w/v). These solutions can greatly assist functional investigations of membrane proteins in the proteomics era. (C) 2011 Elsevier Inc. All rights reserved.

引用

页码：298 / 300

页数：3