Mass spectrometric identification of a candidate biomarker peptide from the in vitro interaction of epichlorohydrin with red blood cells

J Mass Spectrom. 2001 Jan;36(1):47-57. doi: 10.1002/jms.103.

Abstract

The reaction products of epichlorohydrin with human alpha- and beta- globins, obtained through in vitro incubation of these compounds and red blood cells, were determined by using reversed-phase high-performance liquid chromatography (RP-HPLC), electrospray ionization mass spectrometry and matrix-assisted laser desorption/ionization tandem mass spectrometry. The alpha-globin was much more reactive than the beta-globin. At low incubation ratios, approximating the order of magnitude of epichlorohydrin concentration as found in workplaces, the only modified peptide still detectable was the 62-90 belonging to the alpha-chain and carrying an incremental mass of 92 u on either His72 or His89. Given that the two peptides co-eluted in a single chromatographic peak during RP-HPLC separation, they could be chosen as suitable biomarkers for quantification in the setting up of a new methodology for the biological monitoring of persons occupationally exposed, replacing currently known procedures.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Biomarkers / blood*
  • Chromatography, High Pressure Liquid
  • Epichlorohydrin / blood*
  • Erythrocytes / chemistry*
  • Globins / metabolism
  • Humans
  • Mass Spectrometry*
  • Occupational Exposure
  • Peptide Fragments / blood
  • Spectrometry, Mass, Electrospray Ionization
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Trypsin / metabolism

Substances

  • Amino Acids
  • Biomarkers
  • Peptide Fragments
  • Epichlorohydrin
  • Globins
  • Trypsin