title: Sodium laurate, a novel protease- and mass spectrometry-compatible detergent for mass spectrometry-based membrane proteomics.
abstract: The hydrophobic nature of most membrane proteins severely complicates their extraction, proteolysis and identification. Although detergents can be used to enhance the solubility of the membrane proteins, it is often difficult for a detergent not only to have a strong ability to extract membrane proteins, but also to be compatible with the subsequent proteolysis and mass spectrometric analysis. In this study, we made evaluation on a novel application of sodium laurate (SL) to the shotgun analysis of membrane proteomes. SL was found not only to lyse the membranes and solubilize membrane proteins as efficiently as SDS, but also to be well compatible with trypsin and chymotrypsin. Furthermore, SL could be efficiently removed by phase transfer method from samples after acidification, thus ensuring not to interfere with the subsequent CapLC-MS/MS analysis of the proteolytic peptides of proteins. When SL was applied to assist the digestion and identification of a standard protein mixture containing bacteriorhodoposin and the proteins in rat liver plasma membrane-enriched fractions, it was found that, compared with other two representative enzyme- and MS-compatible detergents RapiGest SF (RGS) and sodium deoxycholate (SDC), SL exhibited obvious superiority in the identification of membrane proteins particularly those with high hydrophobicity and/or multiple transmembrane domains.
authors.affiliation: Key Laboratory of Protein Chemistry and Developmental Biology of National Education Committee, College of Life Sciences, Hunan Normal University, Changsha, P R China.
authors.forename: Yong
authors.initials: Y
authors.lastname: Lin
authors.forename: Linju
authors.initials: L
authors.lastname: Huo
authors.forename: Zhonghua
authors.initials: Z
authors.lastname: Liu
authors.forename: Jianglin
authors.initials: J
authors.lastname: Li
authors.forename: Yi
authors.initials: Y
authors.lastname: Liu
authors.forename: Quanze
authors.initials: Q
authors.lastname: He
authors.forename: Xianchun
authors.initials: X
authors.lastname: Wang
authors.forename: Songping
authors.initials: S
authors.lastname: Liang
mesh_terms: D000818:Animals; D001120:Arginine / Q000031:analogs & derivatives / Q000737:chemistry; D002462:Cell Membrane / Q000378:metabolism; D002918:Chymotrypsin / Q000737:chemistry; D019295:Computational Biology; D003840:Deoxycholic Acid / Q000737:chemistry / Q000627:therapeutic use; D003902:Detergents / Q000494:pharmacology*; D007850:Lauric Acids / Q000494:pharmacology*; D008099:Liver / Q000378:metabolism; D013058:Mass Spectrometry; D010447:Peptide Hydrolases / Q000737:chemistry*; D040901:Proteomics; D051381:Rats; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology; D053719:Tandem Mass Spectrometry; D014357:Trypsin / Q000737:chemistry
chemical_list: D003902:Detergents; D007850:Lauric Acids; D003840:Deoxycholic Acid; C030358:lauric acid; D012967:Sodium Dodecyl Sulfate; D001120:Arginine; C009727:benzoylarginine ethyl ester; D010447:Peptide Hydrolases; D002918:Chymotrypsin; D014357:Trypsin
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