Superoxide dismutase,glutathione peroxidase and catalase in oxidative hemolysis. A study of Fanconi's anemia erythrocytes |
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Authors: | I. Mavelli M.R. Ciriolo G. Rotilio P. De Sole M. Castorino A. Stabile |
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Affiliation: | 1. Institute of Biological Chemistry University of Rome Italy;2. CNR Center for Molecular Biology, University of Rome Italy;3. Institute of Biological Chemistry Catholic University, Rome, Italy;4. Department of Paediatrics, Catholic University, Rome, Italy |
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Abstract: | Superoxide dismutase, glutathione peroxidase and catalase were assayed in the erythrocytes of three patients of Fanconi's anemia. Superoxide dismutase was found to be significantly decreased, as previously reported. The enzymes metabolizing H2O2 are normal (glutathione peroxidase in the higher limits of the normal value). The abnormal erythrocytes were found to be as resistant (perhaps more resistant) as normal red blood cells to oxidative hemolysis induced by drugs. Malonyl dialdehyde production was found to be comparable to that of normal erythrocytes. It is concluded that a significant (30–40%) deficiency of superoxide dismutase, when associated to normal values of H2O2-removing enzymes, does not affect the antioxidative defense capability of erythrocytes, even in conditions of augmented oxidative injury. |
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