The present paper deals with the adaptation of the fluorometric measurement of H2O2 originally described by Guilbault et al. (1967, Anal. Chem. 39, 271) for the assay of the peroxisomal oxidation of D-amino acids, L-alpha-hydroxyacids, uric acid, and acyl-CoA esters. The present work essentially covers three facets: (i) the general kinetics of the assay of peroxisomal oxidases and the influence of each component of the assay medium on these kinetics; (ii) the measurement of peroxisomal oxidase activities in subcellular fractions and tissues from human and untreated and clofibrate-treated rodents; and (iii) the comparison between the oxidase activities measured by the fluorometric and spectrophotometric methods.
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