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

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4 引文 斯高帕斯(Scopus)

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.

原文英語
頁(從 - 到)298-300
頁數3
期刊Analytical Biochemistry
418
發行號2
DOIs
出版狀態已發佈 - 2011 十一月 15

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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