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Clinical Chemistry 36: 1339-1343, 1990;
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Clinical Chemistry, Vol 36, 1339-1343, Copyright © 1990 by American Association for Clinical Chemistry

Coupled-enzyme determination of catalase activity in erythrocytes

F Van Lente and M Pepoy
Department of Biochemistry, Cleveland Clinic Foundation, OH 44195.

This coupled-enzyme method for determining the activity of catalase (EC 1.11.1.6) in erythrocyte lysates is based on measuring the absorbance at 340 nm of NADH produced from the peroxidic reaction between ethanol, hydrogen peroxide, and catalase. Hydrogen peroxide is produced as a substrate in situ from the oxidation of glucose catalyzed by glucose oxidase (EC 1.1.3.4). Catalase oxidizes ethanol to acetaldehyde in the presence of hydrogen peroxide. Acetaldehyde is then oxidized by aldehyde dehydrogenase (EC 1.2.1.5) to produce acetate with concomitant conversion of NAD+ to NADH. The reaction did not follow strict zero- order kinetics; enzyme activity was quantified by using initial rates and standards prepared from purified catalase. The method demonstrated within-run and between-run CVs of 1.0% to 2.9% and 2.4% to 3.3%, respectively. This semiautomated method correlated well (r = 0.92) with the more tedious manual method involving measurement at 240 nm.




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