Catalase (CAT) is a vital enzyme found in both animals and plants that detoxifies hydrogen peroxide (H2O2); a major toxic by product of various oxidase and superoxide dismutase activities which if left to accumulate causes the oxidation of cellular targets such as DNA, proteins and lipids resulting into mutagenesis and cell death. CAT activity is inhibited by chemicals like cyanide, ethanol, azide, hydroxylamine, aminotriazole and mercaptoethanol. In this study therefore, we examined the effects of ethanol concentrations and duration of bovine liver catalase (BLC) exposure to Ugandan common sachet alcohol brands (CSAB) on its activity as this is similar to that of humans in function. The concentration of H2O2 ([H2O2]) broken down determined by redox titration using acidified potassium permanganate (KMnO4) was used as a measure of the activity of BLC. The activity decreased with increasing ethanol concentrations, that is, 0.4560±0.0000 mol L-1 at 0% ethanol to 0.2303±0.0125 mol L-1 at 43% ethanol and r2= 94.6%; p= 0.001; and hypothesized to cease within 15 minutes at a 95.45% ethanol. BLC activity also decreased (r2= 69.9%; p= 0.038) with increasing duration of exposure to 40.0% ethanol CSAB from 0.4560±0.0000 mol L-1 at 0 minutes to 0.1475±0.0032 mol L-1 at 25 minutes; and stopped within 34.85 minutes. High ethanol concentrations (> 40%) therefore inactivate BLC as well as 40.0% if incubated in it for longer than 35 minutes. We therefore postulate that the Ugandan CSAB of 37-43% ethanol sold on the open markets in Uganda should not be consumed in large quantities continuously for more than 35 minutes as this may be lethal.