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1965•Canadian Journal of BiochemistryRequires access

ERYTHROCYTE CATALASE AND DETOXICATION OF HYDROGEN PEROXIDE

N. V. Paniker, G. Y. N. Iyer

Open publisher page 36 citations

Abstract

Erythrocytes from several animal species with widely differing catalase levels were exposed to H2O2and the susceptibility of Hb to oxidation measured. In the absence of glucose the rapidity of MHb formation was inversely related to the catalase activity and directly related to the concentration of H2O2attained. Added catalase or hemolysates of catalase-rich erythrocytes counteracted the effect of H2O2, while azide rendered Hb of even catalase-rich cells susceptible to rapid oxidation. Added glucose largely prevented the formation of MHb on exposure to H2O2; this protective effect was less marked in azide-treated cells than in control cells. These results suggest that catalase complements the protective action of glucose and thereby regulates MHb formation and accumulation in erythrocytes.

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What this paper is about

Erythrocytes from several animal species with widely differing catalase levels were exposed to H2O2and the susceptibility of Hb to oxidation measured. In the absence of glucose the rapidity of MHb formation was inversely related to the catalase activity and directly related to the concentration of H2O2attained. Added catalase or hemolysates of catalase-rich erythrocytes counteracted the effect of H2O2, while azide rendered Hb of even catalase-rich cells susceptible to rapid oxidation. Added glucose largely prevented the formation of MHb on exposure to H2O2; this protective effect was less marked in azide-treated cells than in control cells. These results suggest that catalase complements the protective action of glucose and thereby regulates MHb formation and accumulation in erythrocytes.

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Available abstract

Erythrocytes from several animal species with widely differing catalase levels were exposed to H2O2and the susceptibility of Hb to oxidation measured. In the absence of glucose the rapidity of MHb formation was inversely related to the catalase activity and directly related to the concentration of H2O2attained. Added catalase or hemolysates of catalase-rich erythrocytes counteracted the effect of H2O2, while azide rendered Hb of even catalase-rich cells susceptible to rapid oxidation. Added glucose largely prevented the formation of MHb on exposure to H2O2; this protective effect was less marked in azide-treated cells than in control cells. These results suggest that catalase complements the protective action of glucose and thereby regulates MHb formation and accumulation in erythrocytes.

Key concepts: Catalase, Hydrogen peroxide, Sodium azide, Chemistry, Azide, Biochemistry, Enzyme, Detoxication

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ERYTHROCYTE CATALASE AND DETOXICATION OF HYDROGEN PEROXIDE — Research Paper | ScholarLens