Oxidative modification of tryptophan residues exposed to peroxynitrite.

Y Kato, S Kawakishi, T Aoki, K Itakura, T Osawa

文献索引：Biochem. Biophys. Res. Commun. 234(1) , 82-4, (1997)

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摘要

The aim of this study was to clarify the mechanism of loss of Trp residues in proteins exposed to peroxynitrite. The Trp residues in bovine serum albumin and collagen IV were decreased by peroxynitrite treatment. To identify the degradation products of the Trp residue by peroxynitrite, tert-butoxycarbonyl-L-tryptophan (Boc-Trp) was used as a model of the Trp residue in proteins, and the products formed from peroxynitrite-treated Boc-Trp were then isolated. Boc-Trp decreased with an increase in peroxynitrite concentration. N-Formylkynurenine, oxindole, and hydropyrroloindole were identified as major products. The formation of these products may account for the losses of Trp residues in proteins by peroxynitrite.