Removal of detergents from protein digests for mass spectrometry analysis

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

doi:10.1016/j.ab.2008.07.034

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 journal › Article › peer-review

80 Scopus citations

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 language	English (US)
Pages (from-to)	135-137
Number of pages	3
Journal	Analytical Biochemistry
Volume	382
Issue number	2
DOIs	https://doi.org/10.1016/j.ab.2008.07.034
State	Published - Nov 15 2008

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.ab.2008.07.034

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title = "Removal of detergents from protein digests for mass spectrometry analysis",

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.",

author = "Yeung, {Yee Guide} and Edward Nieves and Angeletti, {Ruth Hogue} and Stanley, {E. Richard}",

note = "Funding Information: This work was supported by National Institutes of Health Grants CA26504 (E.R.S.) and CA101150 (R.H.A.) and Albert Einstein College of Medicine Cancer Center Grant 5P30-CA13330. ",

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AU - Yeung, Yee Guide

AU - Nieves, Edward

AU - Angeletti, Ruth Hogue

AU - Stanley, E. Richard

N1 - Funding Information: This work was supported by National Institutes of Health Grants CA26504 (E.R.S.) and CA101150 (R.H.A.) and Albert Einstein College of Medicine Cancer Center Grant 5P30-CA13330.

PY - 2008/11/15

Y1 - 2008/11/15

N2 - 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.

AB - 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.

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JO - Analytical Biochemistry

JF - Analytical Biochemistry

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ER -

Removal of detergents from protein digests for mass spectrometry analysis

Abstract

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