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Catalase and glutathione peroxidase are equally active in detoxification of
hydrogen peroxide in human erythrocytes
GF Gaetani, S Galiano, L Canepa, AM Ferraris and HN Kirkman
Division of Hematology, University of Genoa, Italy.
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.
Volume 73,
Issue 1,
pp. 334-339,
01/01/1989
Copyright © 1989 by The American Society of Hematology
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