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 |
Fingerprint
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 journal › Article
}
TY - JOUR
T1 - Optimal concentrations of N-decanoyl-N-methylglucamine and sodium dodecyl sulfate allow the extraction and analysis of membrane proteins
AU - Chuang, Jen Hua
AU - Kao, Yu Jing
AU - Ruderman, Neil B.
AU - Tung, Li Chu
AU - Lin, Yenshou
PY - 2011/11/15
Y1 - 2011/11/15
N2 - 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.
AB - 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.
KW - CMC
KW - Integral membrane proteins
KW - MEGA-10
KW - Membrane proteins
KW - SDS
UR - http://www.scopus.com/inward/record.url?scp=80052700273&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=80052700273&partnerID=8YFLogxK
U2 - 10.1016/j.ab.2011.08.006
DO - 10.1016/j.ab.2011.08.006
M3 - Article
C2 - 21871431
AN - SCOPUS:80052700273
VL - 418
SP - 298
EP - 300
JO - Analytical Biochemistry
JF - Analytical Biochemistry
SN - 0003-2697
IS - 2
ER -