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In this investigation, the effects of azinphosmethyl and dimethoate on bovine liver catalase were searched. The catalase enzyme activity values were measured by the interaction of the catalase with azinphos-methyl and dimethoate prepared at concentrations of from 0 to 500 mg / L. The catalase enzyme activity sharply decreased while azinphos-methyl concentration increased. An irreversible inhibition was determined in the catalase activity which interacts with azinphos-methyl. However, following dimethoate application, the catalase activity showed a decline at concentrations of 25, 50 and 100 mg / L of dimethoate and an elevation at concentrations of 250 and 500 mg / L of dimethoate. The catalase behaved differently according to varying concentrations of dimethoate with inhibitions at low concentrations and activations at high concentrations.