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.
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页码：298 / 300
页数：3
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