Literature DB >> 20155730

Rapid detergent removal from peptide samples with ethyl acetate for mass spectrometry analysis.

Yee-Guide Yeung1, E Richard Stanley.   

Abstract

Detergents are required for the extraction of hydrophobic proteins and for the maintenance of their solubility in solution. However, the presence of detergents in the peptide samples severely suppresses ionization in mass spectrometry (MS) analysis and decreases chromatographic resolution in LC-MS. Thus, detergents must be removed for sensitive detection of peptides by MS. This unit describes a rapid protocol in which ethyl acetate extraction is used to remove octylglucoside from protease digests without loss of peptides. This procedure can also be used to reduce interference by sodium dodecyl sulfate, Nonidet P-40, or Triton X-100 in peptide samples for MS analysis.

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Year:  2010        PMID： 20155730      PMCID： PMC2852680          DOI： 10.1002/0471140864.ps1612s59

Source DB:  PubMed          Journal:  Curr Protoc Protein Sci        ISSN： 1934-3655


  10 in total

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Authors:  H Katayama; T Nagasu; Y Oda
Journal:  Rapid Commun Mass Spectrom       Date:  2001       Impact factor: 2.419

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7.  Effects of common surfactants on protein digestion and matrix-assisted laser desorption/ionization mass spectrometric analysis of the digested peptides using two-layer sample preparation.

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Journal:  Rapid Commun Mass Spectrom       Date:  2004       Impact factor: 2.419

8.  Acid-labile surfactant improves in-sodium dodecyl sulfate polyacrylamide gel protein digestion for matrix-assisted laser desorption/ionization mass spectrometric peptide mapping.

Authors:  Eiko Nomura; Kazuhiro Katsuta; Tomoko Ueda; Michinori Toriyama; Tatsuya Mori; Naoyuki Inagaki
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9.  Removal of detergents from protein digests for mass spectrometry analysis.

Authors:  Yee-Guide Yeung; Edward Nieves; Ruth Hogue Angeletti; E Richard Stanley
Journal:  Anal Biochem       Date:  2008-08-03       Impact factor: 3.365

10.  Phase transfer surfactant-aided trypsin digestion for membrane proteome analysis.

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  10 in total
  25 in total

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3.  Novel, gel-free proteomics approach identifies RNF5 and JAMP as modulators of GPCR stability.

Authors:  Sébastien J Roy; Irina Glazkova; Louis Fréchette; Christian Iorio-Morin; Chantal Binda; Darlaine Pétrin; Phan Trieu; Mélanie Robitaille; Stéphane Angers; Terence E Hébert; Jean-Luc Parent
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