Structural analysis of naphthoquinone protein adducts with liquid chromatography/tandem mass spectrometry and the scoring algorithm for spectral analysis (SALSA).

摘要: The relative reactivities of various naphthoquinone isomers (1,4-, 1,2- and 2-methyl-1,4-naphthoquinone) to two test proteins, apomyoglobin human hemoglobin, were evaluated via liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS). structural characterization the resulting adducts was also obtained by LC/ESI-MS analysis intact proteins. reactive sites hemoglobin with 1,4-naphthoquinone 1,2-naphthoquinone identified through adducted tryptic peptides use high-pressure tandem (HPLC/ESI-MS/MS), TurboSEQUEST, scoring algorithm for spectral (SALSA). Four peptides, which formed nucleophilic addition a lysine amino acid residue 1,4-naphthoquinone, identified, as an peptide from incubation apomyoglobin. In case naphthoquinones, N-terminal valine modification alpha beta chains hemoglobin. protein formation may imply that naphthalene produces its in vivo toxicity metabolites reacting biomolecular