Analytical Biochemistry 2011-11-15

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

Jen-Hua Chuang, Yu-Jing Kao, Neil B Ruderman, Li-Chu Tung, Yenshou Lin

文献索引：Anal. Biochem. 418(2) , 298-300, (2011)

全文：HTML全文

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.Copyright © 2011 Elsevier Inc. All rights reserved.