Suppression of catalase activity by peroxidase and its substrates

Abstract
H2O2 added to wheat-germ suspension containing catalase, peroxidase and a substrate of the latter was preferentially used by peroxidase in the oxidation of the substrate. Catalase activity was largely suppressed while the oxidation of the substrate proceeded. In systems composed of wheat germ and horse liver cat alase, and horse liver catalase and horse-radish (peroxidase), the extent of this suppression in the other systems studied, the extent of this suppression was found to depend on the concn. of the enzymes as well as on the ratio of their activities. The peroxidase substrates tested damaged catalase activity, but were much less injurious in presence of peroxidase.