UNIT 17.9 Identification and Characterization of Oxylipid-Protein and Peptide Conjugates by Mass Spectrometry

  1. Woon-Gye Chung,
  2. Claudia S. Maier

Published Online: 1 FEB 2008

DOI: 10.1002/0471140856.tx1709s35

Current Protocols in Toxicology

Current Protocols in Toxicology

How to Cite

Chung, W.-G. and Maier, C. S. 2008. Identification and Characterization of Oxylipid-Protein and Peptide Conjugates by Mass Spectrometry. Current Protocols in Toxicology. 35:17.9:17.9.1–17.9.19.

Author Information

  1. Oregon State University, Department of Chemistry, Corvallis, Oregon

Publication History

  1. Published Online: 1 FEB 2008
  2. Published Print: FEB 2008


The modification of proteins by reactive products of lipid peroxidation is associated with a large number of diseases and biological aging; thus, methods that enable the characterization of oxylipid-protein and/or peptide conjugates are highly in demand. This unit outlines a chemical labeling approach to identifying and characterizing proteins modified by lipid peroxidation products. It also outlines two approaches for mass spectrometry–based identification and detailed characterization of oxylipid conjugates. The first combines chemical labeling of oxylipid-protein conjugates using an aldehyde-specific biotinylation reagent, electrophoretic separation, and mass spectrometry–based identification of the biotinylated proteins. In the second approach, protein extracts are treated with the aldehyde-specific reagent, proteolyzed using trypsin, and the biotinylated peptides are enriched using immobilized monomeric avidin. The enriched peptide fractions are submitted to tandem mass spectrometry for determining the peptide sequence information, site of the modification, and chemical nature of the oxylipid. Curr. Protoc. Toxicol. 35:17.9.1-17.9.19. © 2008 by John Wiley & Sons, Inc.


  • lipid peroxidation;
  • oxylipid;
  • chemical labeling;
  • mass spectrometry