@article{06943b74de3e43fb9146e8b29ed1b920,
title = "Optimal concentrations of N-decanoyl-N-methylglucamine and sodium dodecyl sulfate allow the extraction and analysis of membrane proteins",
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.",
keywords = "CMC, Integral membrane proteins, MEGA-10, Membrane proteins, SDS",
author = "Chuang, {Jen Hua} and Kao, {Yu Jing} and Ruderman, {Neil B.} and Tung, {Li Chu} and Yenshou Lin",
note = "Funding Information: This work was partially supported by a Grant ( NSC98-2311-B-003-MY3 ) to Y. Lin from the National Science Council, Taiwan . We are grateful for the support ( 98031015 and 99031021 ) of the Office of Research and Development, National Taiwan Normal University, Taiwan . We thank Dr. Dennis J.-Y. Hsieh for technical assistance. ",
year = "2011",
month = nov,
day = "15",
doi = "10.1016/j.ab.2011.08.006",
language = "English",
volume = "418",
pages = "298--300",
journal = "Analytical Biochemistry",
issn = "0003-2697",
publisher = "Academic Press Inc.",
number = "2",
}