The effect of the peroxide concentration and other factors on the decomposition of hydrogen peroxide by catalase

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Abstract
The evolution of oxygen from H2O2 at pH 5.58 by liver catalase, erythrocyte catalase and a suspension of plasmolyzed red blood corpuscles was measured manometrically and by the "boat technique" using a pressure gauge for following rapid rates. There was an initial rapid evolution of O2 followed by a slower steady evolution: a transition from alpha- to beta-activity. Identical kinetic relationships were obtained with the 3 specimen of catalase. The rate was directly proportional to the catalase concn. The rate variation with peroxide concn. showed a max. at about 0.07 [image] H2O2- The enzyme distinction, purity of the enzyme, the pressure of inhibitors, or the buffer soln. used did not determine kinetic relationships. Dilution during the period of initial rapid activity showed a similar reversibility which suggested that the transition from alpha- to beta-activity was not caused by partial enzyme destruction.