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

Yee Guide Yeung, E. Richard Stanley

Research output: Contribution to journalArticle

20 Citations (Scopus)

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.

Original languageEnglish (US)
JournalCurrent Protocols in Protein Science
Issue numberSUPPL. 59
DOIs
StatePublished - 2010

Fingerprint

Detergents
Mass spectrometry
Mass Spectrometry
Peptides
Octoxynol
Sodium Dodecyl Sulfate
Solubility
Ionization
Peptide Hydrolases
Maintenance
ethyl acetate
Proteins

Keywords

  • Detergent removal
  • Ethyl acetate extraction
  • Mass spectrometry
  • Octylglucoside

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology

Cite this

Rapid detergent removal from peptide samples with ethyl acetate for mass spectrometry analysis. / Yeung, Yee Guide; Stanley, E. Richard.

In: Current Protocols in Protein Science, No. SUPPL. 59, 2010.

Research output: Contribution to journalArticle

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