Interference of carbidopa and other catechols with reactions catalyzed by peroxidases

Publication date: July 2018
Source:Biochimica et Biophysica Acta (BBA) – General Subjects, Volume 1862, Issue 7
Author(s): Beata Gąsowska-Bajger, Yuki Nishigaya, Krystyna Hirsz-Wiktorzak, Anna Rybczyńska, Toshimasa Yamazaki, Hubert Wojtasek
BackgroundA number of compounds, including ascorbic acid, catecholamines, flavonoids, p-diphenols and hydrazine derivatives have been reported to interfere with peroxidase-based medical diagnostic tests (Trinder reaction) but the mechanisms of these effects have not been fully elucidated.MethodsReactions of bovine myeloperoxidase with o-dianisidine, bovine lactoperoxidase with ABTS and horseradish peroxidase with 4-aminoantipyrine/phenol in the presence of carbidopa, an anti-Parkinsonian drug, and other catechols, including l-dopa, were monitored spectrophotometrically and by measuring hydrogen peroxide consumption.ResultsChromophore formation in all three enzyme/substrate systems was blocked in the presence of carbidopa and other catechols. However, the rates of hydrogen peroxide consumption were not much affected. Irreversible enzyme inhibition was also insignificant.ConclusionsTested compounds reduced the oxidation products or intermediates of model substrates thus preventing chromophore formation. This interference may affect interpretation of results of diagnostic tests in samples from patients with Parkinson’s disease treated with carbidopa and l-dopa.General significanceThis mechanism allows prediction of interference in peroxidase-based diagnostic tests for other compounds, including drugs and natural products.

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