作者: Marilyn Ehrenshaft , Sueli de Oliveira Silva , Irina Perdivara , Piotr Bilski , Robert H. Sik
DOI: 10.1016/J.FREERADBIOMED.2009.01.020
关键词:
摘要: Reactions of tryptophan residues in proteins with radical and other oxidative species frequently lead to cleavage the indole ring, modifying into N-formylkynurenine (NFK) kynurenine. Tryptophan modification has been detected physiologically important associated a number human disease conditions. Modified have identified through various combinations proteomic analyses, tryptic digestion, HPLC, mass spectrometry. Here we present novel, immunological approach using polyclonal antiserum for detection NFK. The specificity our is confirmed photooxidation radical-mediated oxidation without residues. sensitivity validated NFK photooxidized myoglobin (two residues) carbonate radical-oxidized SOD1, which contains single residue. Analysis milk also shows that can detect mixture proteins. Results from spectrometric analysis samples corroborate data, detecting an increase content as extent increases.