Ian Max Møller

Optimized biotin-hydrazide enrichment and mass spectrometry analysis of peptide carbonyls

Publikation: KonferencebidragPosterForskning

  • Jesper F. Havelund, Danmark
  • K Wojdyla, University of Southern Denmark, Danmark
  • O. N. Jensen, University of Southern Denmark, Danmark
  • Ian Max Møller
  • A. Rogowska-Wrzesinska, Institut for Biokemi og Molekylær Biologi
Irreversible cell damage through protein carbonylation is the result of reaction with reactive oxygen species (ROS) and has been coupled to many diseases. The precise molecular consequences of protein carbonylation, however, are still not clear. The localization of the carbonylated amino acid is an important piece of information in this puzzle. Mass spectrometry is here a superior tool; however, protein/peptide carbonylation is of low stoichiometry and the MS signal is decreased due to low ionization efficiency and signal suppression from non-modified peptides. In addition, other more common modifications are isobaric to carbonylation and it is often challenging to detect the weaker signal from carbonylated peptides necessitating enrichment step. We here present an optimized method for the enrichment of carbonylated peptides.
Udgivelsesår6 okt. 2014
StatusUdgivet - 6 okt. 2014
BegivenhedHuman proteome organization World congress: The proteome quest to understand biology and disease - Madrid, Spanien
Varighed: 6 okt. 20149 okt. 2014
Konferencens nummer: 13


KonferenceHuman proteome organization World congress

Se relationer på Aarhus Universitet Citationsformater

ID: 84333311