Effective Removal of Nonionic Detergents in Protein Mass Spectrometry, Hydrogen/Deuterium Exchange, and Proteomics. Rey, M., Mrazek, H., Pompach, P., Novak, P., Pelosi, L., Brandolin, G., Forest, E., Havlicek, V., & Man, P. Anal. Chem. (Washington, DC, United States), 82(12):5107–5116, 2010.
doi  abstract   bibtex   
Detergents are frequently used for protein isolation and solubilization. Their presence is crucial in membrane protein protocols or in lipid raft proteomics. However, they are usually poorly compatible with mass spectrometry. Several different sample prepn. protocols are routinely used, but they are either laborious or suffer from sample losses. Here, we describe our alternative method for nonionic detergent removal. It is based on selective detergent extn. after capture of the sample on a reversed phase cartridge. The extn. is performed by chlorinated solvents and works well for polyoxyethylene based nonionic detergents, but also for polymers like polyethylene and propylene glycol. Detergent removal can be also carried out on the protein level but a special care must be taken with hydrophobic proteins. In such cases, it is preferable to perform detergent removal after proteolysis which digests the protein to peptides and reduces the hydrophobicity. The method can easily be automated and is compatible with hydrogen/deuterium exchange coupled to mass spectrometry. [on SciFinder(R)]
@article{ rey_effective_2010,
  title = {Effective Removal of Nonionic Detergents in Protein Mass Spectrometry, {Hydrogen/Deuterium} Exchange, and Proteomics.},
  volume = {82},
  issn = {0003-2700},
  doi = {10.1021/ac100171m},
  abstract = {Detergents are frequently used for protein isolation and solubilization. Their presence is crucial in membrane protein protocols or in lipid raft proteomics. However, they are usually poorly compatible with mass spectrometry. Several different sample prepn. protocols are routinely used, but they are either laborious or suffer from sample losses. Here, we describe our alternative method for nonionic detergent removal. It is based on selective detergent extn. after capture of the sample on a reversed phase cartridge. The extn. is performed by chlorinated solvents and works well for polyoxyethylene based nonionic detergents, but also for polymers like polyethylene and propylene glycol. Detergent removal can be also carried out on the protein level but a special care must be taken with hydrophobic proteins. In such cases, it is preferable to perform detergent removal after proteolysis which digests the protein to peptides and reduces the hydrophobicity. The method can easily be automated and is compatible with hydrogen/deuterium exchange coupled to mass spectrometry. [on {SciFinder(R)]}},
  number = {12},
  journal = {Anal. Chem. (Washington, {DC}, United States)},
  author = {Rey, Martial and Mrazek, Hynek and Pompach, Petr and Novak, Petr and Pelosi, Ludovic and Brandolin, Gerard and Forest, Eric and Havlicek, Vladimir and Man, Petr.},
  year = {2010},
  keywords = {detergent, deuterium, exchange, hydrogen, mass, nonionic, proteomics, removal, spectrometry},
  pages = {5107–5116}
}

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