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 language | English |
|---|---|
| Pages (from-to) | 298-300 |
| Number of pages | 3 |
| Journal | Analytical Biochemistry |
| Volume | 418 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2011 Nov 15 |
Keywords
- CMC
- Integral membrane proteins
- MEGA-10
- Membrane proteins
- SDS
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
Fingerprint Dive into the research topics of 'Optimal concentrations of N-decanoyl-N-methylglucamine and sodium dodecyl sulfate allow the extraction and analysis of membrane proteins'. Together they form a unique fingerprint.
Cite this
Chuang, J. H., Kao, Y. J., Ruderman, N. B., Tung, L. C., & Lin, Y. (2011). Optimal concentrations of N-decanoyl-N-methylglucamine and sodium dodecyl sulfate allow the extraction and analysis of membrane proteins. Analytical Biochemistry, 418(2), 298-300. https://doi.org/10.1016/j.ab.2011.08.006