Abstract
Rates of oxidation of bilirubin species were determined spectrometrically using enzymatic oxidation of bilirubin by peroxidase (POD: EC 1.11.1.7) and hydrogen peroxide. Rates of oxidation of conjugated and unconjugated bilirubin (Bc and Bu) were examined with and without serum albumin and compared, and those of bilirubin bound covalently to albumin were determined using naturally occurring delta-bilirubin (Bd). In the presence of serum albumin (Alb), Bc-Alb showed the highest rate of oxidation by POD oxidation followed by Bu-Alb and Bd. Without serum albumin Bu showed a higher rate of oxidation than Bc, despite the fact that Bc exerted more interference than Bu on the enzymatic determination of uric acid (coupled with POD reaction and dye formation).
