Oxidative damage to protein is associated with the pathogenesis of several diseases and physiological processes such as aging, ischemia-reperfusion injury, and protein turn-over. Allysine, a deaminated lysine residue of protein, is highly reactive and hydrophobic inducing protein cross-links by Schiff base formation or aldol condensation. Benzylamine was oxidatively deaminated to benzaldehyde by both H2O2/Cu2+ and ascorbic acid/Cu2+ systems (pH 7.4), with and without aspirin. Reaction mixture was quenched using 2 ml 1 mM Acetic acid. The resulting benzaldehyde was measured spectrophotometrically at 245 nm. Aspirin increased the production of benzaldehyde in both systems.

KEYWORDS: Aspirin; Benzylamine; Benzaldehyde; Free radical; Oxidative deamination; Metal-Catalyzed deamination.