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

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)298-300
Number of pages3
JournalAnalytical Biochemistry
Volume418
Issue number2
DOIs
Publication statusPublished - 2011 Nov 15

Fingerprint

Meglumine
Sodium Dodecyl Sulfate
Detergents
Buffers
Membrane Proteins
Critical micelle concentration
Micelles
Electrophoresis
Proteomics
Proteins
Western Blotting
decanoyl-N-methylglucamide

Keywords

  • CMC
  • Integral membrane proteins
  • MEGA-10
  • Membrane proteins
  • SDS

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Optimal concentrations of N-decanoyl-N-methylglucamine and sodium dodecyl sulfate allow the extraction and analysis of membrane proteins. / Chuang, Jen Hua; Kao, Yu Jing; Ruderman, Neil B.; Tung, Li Chu; Lin, Yenshou.

In: Analytical Biochemistry, Vol. 418, No. 2, 15.11.2011, p. 298-300.

Research output: Contribution to journalArticle

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