Removal of detergents from protein digests for mass spectrometry analysis

Yee Guide Yeung, Edward Nieves, Ruth Hogue Angeletti, E. Richard Stanley

Research output: Contribution to journalArticle

55 Citations (Scopus)

Abstract

Detergents are commonly used for the extraction of hydrophobic proteins and must be removed for sensitive detection of peptides by mass spectrometry. We demonstrate that ethyl acetate is able to extract octylglycoside from a protease digest without loss of peptides or interference with the peptide mass spectral profile. Ethyl acetate extraction was also found to reduce interference by sodium dodecyl sulfate, Nonidet P-40, or Triton X-100 in the mass spectrometry analysis.

Original languageEnglish (US)
Pages (from-to)135-137
Number of pages3
JournalAnalytical Biochemistry
Volume382
Issue number2
DOIs
StatePublished - Nov 15 2008

Fingerprint

Detergents
Mass spectrometry
Mass Spectrometry
Peptides
Proteins
Octoxynol
Sodium Dodecyl Sulfate
Peptide Hydrolases
ethyl acetate
Nonidet P-40

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Removal of detergents from protein digests for mass spectrometry analysis. / Yeung, Yee Guide; Nieves, Edward; Angeletti, Ruth Hogue; Stanley, E. Richard.

In: Analytical Biochemistry, Vol. 382, No. 2, 15.11.2008, p. 135-137.

Research output: Contribution to journalArticle

Yeung, Yee Guide ; Nieves, Edward ; Angeletti, Ruth Hogue ; Stanley, E. Richard. / Removal of detergents from protein digests for mass spectrometry analysis. In: Analytical Biochemistry. 2008 ; Vol. 382, No. 2. pp. 135-137.
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