Optimal concentrations of N-decanoyl-N-methylglucamine and sodium dodecyl sulfate allow the extraction and analysis of membrane proteins.
Anal Biochem
; 418(2): 298-300, 2011 Nov 15.
Article
en En
| MEDLINE
| ID: mdl-21871431
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.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Dodecil Sulfato de Sodio
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Tensoactivos
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Ácidos Grasos
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Glucosamina
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Proteínas de la Membrana
Límite:
Humans
Idioma:
En
Año:
2011
Tipo del documento:
Article