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

doi:10.1016/j.ab.2011.08.006

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

Department of Life Science

Research output: Contribution to journal › Article › peer-review

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 language	English
Pages (from-to)	298-300
Number of pages	3
Journal	Analytical Biochemistry
Volume	418
Issue number	2
DOIs	https://doi.org/10.1016/j.ab.2011.08.006
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

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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. Copyright: Copyright 2020 Elsevier B.V., All rights reserved.",

year = "2011",

month = nov,

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doi = "10.1016/j.ab.2011.08.006",

language = "English",

volume = "418",

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journal = "Analytical Biochemistry",

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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

N1 - 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. Copyright: Copyright 2020 Elsevier B.V., All rights reserved.

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

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JO - Analytical Biochemistry

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ER -

Optimal concentrations of N-decanoyl-N-methylglucamine and sodium dodecyl sulfate allow the extraction and analysis of membrane proteins

Abstract

Keywords

ASJC Scopus subject areas

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