Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes.
Article Details
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Gaetani GF, Galiano S, Canepa L, Ferraris AM, Kirkman HN
Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes.
Blood. 1989 Jan;73(1):334-9.
- PubMed ID
- 2491951 [ View in PubMed]
- Abstract
Genetic deficiencies of glucose-6-phosphate dehydrogenase (G6PD) and NADPH predispose affected erythrocytes to destruction from peroxides. Conversely, genetic deficiencies of catalase do not predispose affected erythrocytes to peroxide-induced destruction. These observations have served to strengthen the assumption that the NADPH/glutathione/glutathione peroxidase pathway is the principal means for disposal of H2O2 in human erythrocytes. Recently, however, mammalian catalase was found to have tightly bound NADPH and to require NADPH for the prevention and reversal of inactivation by its toxic substrate (H2O2). Since both catalase and the glutathione pathway are dependent on NADPH for function, this finding raises the possibility that both mechanisms destroy H2O2 in human erythrocytes. A comparison of normal and acatalasemic erythrocytes in the present study indicated that catalase accounts for more than half of the destruction of H2O2 when H2O2 is generated at a rate comparable to that which leads to hemolysis in G6PD- deficient erythrocytes.
DrugBank Data that Cites this Article
- Drug Enzymes
Drug Enzyme Kind Organism Pharmacological Action Actions Hydrogen peroxide Catalase Protein Humans UnknownSubstrateDetails Hydrogen peroxide Glutathione peroxidase 1 Protein Humans UnknownSubstrateDetails - Drug Reactions
Reaction Details
