Mass spectrometric identification of a candidate biomarker peptide from the in vitro interaction of epichlorohydrin with red blood cells
✍ Scribed by Nadia Miraglia; Gabriella Pocsfalvi; Pasquale Ferranti; Adriana Basile; Nicola Sannolo; Antonio Acampora; Leonardo Soleo; Ferdinando Palmieri; Simonetta Caira; Beatrice De Giulio; Antonio Malorni
- Publisher
- John Wiley and Sons
- Year
- 2001
- Tongue
- English
- Weight
- 269 KB
- Volume
- 36
- Category
- Article
- ISSN
- 1076-5174
- DOI
- 10.1002/jms.103
No coin nor oath required. For personal study only.
✦ Synopsis
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.