Removal of detergents from protein digests for mass spectrometry analysis.
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.
Yeung
Yee-Guide
YG
Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Nieves
Edward
E
Angeletti
Ruth Hogue
RH
Stanley
E Richard
ER
D000085:Acetates / Q000737:chemistry; D003902:Detergents / Q000302:isolation & purification*; D010455:Peptides / Q000032:analysis / Q000737:chemistry; D011506:Proteins / Q000737:chemistry / Q000302:isolation & purification*; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013501:Surface-Active Agents / Q000737:chemistry / Q000302:isolation & purification
D000085:Acetates; D003902:Detergents; D010455:Peptides; D011506:Proteins; D013501:Surface-Active Agents; D012967:Sodium Dodecyl Sulfate; C007650:ethyl acetate