Unit

UNIT 16.12 Rapid Detergent Removal from Peptide Samples with Ethyl Acetate for Mass Spectrometry Analysis

  1. Yee-Guide Yeung,
  2. E. Richard Stanley1

Published Online: 1 FEB 2010

DOI: 10.1002/0471140864.ps1612s59

Current Protocols in Protein Science

Current Protocols in Protein Science

How to Cite

Yeung, Y.-G. and Stanley, E. R. 2010. Rapid Detergent Removal from Peptide Samples with Ethyl Acetate for Mass Spectrometry Analysis. Current Protocols in Protein Science. 59:16.12:16.12.1–16.12.5.

Author Information

  1. 1

    Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, New York

Publication History

  1. Published Online: 1 FEB 2010
  2. Published Print: FEB 2010

Abstract

Detergents are required for the extraction of hydrophobic proteins and for the maintenance of their solubility in solution. However, the presence of detergents in the peptide samples severely suppresses ionization in mass spectrometry (MS) analysis and decreases chromatographic resolution in LC-MS. Thus, detergents must be removed for sensitive detection of peptides by MS. This unit describes a rapid protocol in which ethyl acetate extraction is used to remove octylglucoside from protease digests without loss of peptides. This procedure can also be used to reduce interference by sodium dodecyl sulfate, Nonidet P-40, or Triton X-100 in peptide samples for MS analysis. Curr. Protoc. Protein Sci. 59:16.12.1-16.12.5. © 2010 by John Wiley & Sons, Inc.

Keywords:

  • detergent removal;
  • mass spectrometry;
  • ethyl acetate extraction;
  • octylglucoside