Kinetics of bilirubin oxidation with peroxidase, as applied to studies of bilirubin-albumin binding

Scand J Clin Lab Invest. 1979 Apr;39(2):143-50. doi: 10.1080/00365517909106086.

Abstract

In the determination of unbound bilirubin by rate of oxidation with peroxidase, errors may be caused by (1) phenol, propylparaben, and phenothiazines (free radical acceleration), (2) haemoglobin (peroxidase effect), and (3) ascorbate (inhibition). Such errors may be diminished by dilution 1:40, or with an anti-oxidant, tert-butyl-p-hydroxyanisole, and ascorbate oxidase.

MeSH terms

  • Ascorbate Oxidase / pharmacology
  • Bilirubin / metabolism*
  • Hemoglobins / analysis
  • Humans
  • Kinetics
  • Oxidation-Reduction
  • Parabens / antagonists & inhibitors
  • Peroxidases / pharmacology*
  • Phenols / antagonists & inhibitors
  • Phenothiazines / antagonists & inhibitors
  • Protein Binding / drug effects
  • Serum Albumin / metabolism*

Substances

  • Hemoglobins
  • Parabens
  • Phenols
  • Phenothiazines
  • Serum Albumin
  • Ascorbate Oxidase
  • Peroxidases
  • Bilirubin