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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.

SUBMITTER: Yeung YG 

PROVIDER: S-EPMC2584337 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature

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Removal of detergents from protein digests for mass spectrometry analysis.

Yeung Yee-Guide YG   Nieves Edward E   Angeletti Ruth Hogue RH   Stanley E Richard ER  

Analytical biochemistry 20080803 2


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. ...[more]

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