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Title: Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes

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 H/sub 2/O/sub 2/ 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 (H/sub 2/O/sub 2/). Since both catalase and the glutathione pathway are dependent on NADPH for function, this finding raises the possibility that both mechanisms destroy H/sub 2/O/sub 2/ 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 H/sub 2/O/sub 2/ when H/sub 2/O/sub 2/ is generated at a rate comparable to that which leads to hemolysis in G6PD- deficient erythrocytes.

Authors:
; ; ; ;
Publication Date:
Research Org.:
Univ. of Genoa (Italy)
OSTI Identifier:
6402670
Resource Type:
Journal Article
Journal Name:
Blood; (United States)
Additional Journal Information:
Journal Volume: 73:1
Country of Publication:
United States
Language:
English
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; CATALASE; ENZYME ACTIVITY; HYDROGEN PEROXIDE; DETOXIFICATION; PEROXIDASES; BIOLOGICAL PATHWAYS; CARBON DIOXIDE; ERYTHROCYTES; MAN; NAD; ANIMALS; BIOLOGICAL MATERIALS; BLOOD; BLOOD CELLS; BODY FLUIDS; CARBON COMPOUNDS; CARBON OXIDES; CHALCOGENIDES; COENZYMES; ENZYMES; HYDROGEN COMPOUNDS; MAMMALS; MATERIALS; NUCLEOTIDES; ORGANIC COMPOUNDS; OXIDES; OXIDOREDUCTASES; OXYGEN COMPOUNDS; PEROXIDES; PRIMATES; VERTEBRATES; 560300* - Chemicals Metabolism & Toxicology

Citation Formats

Gaetani, G F, Galiano, S, Canepa, L, Ferraris, A M, and Kirkman, H N. Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes. United States: N. p., 1989. Web.
Gaetani, G F, Galiano, S, Canepa, L, Ferraris, A M, & Kirkman, H N. Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes. United States.
Gaetani, G F, Galiano, S, Canepa, L, Ferraris, A M, and Kirkman, H N. 1989. "Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes". United States.
@article{osti_6402670,
title = {Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes},
author = {Gaetani, G F and Galiano, S and Canepa, L and Ferraris, A M and Kirkman, H N},
abstractNote = {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 H/sub 2/O/sub 2/ 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 (H/sub 2/O/sub 2/). Since both catalase and the glutathione pathway are dependent on NADPH for function, this finding raises the possibility that both mechanisms destroy H/sub 2/O/sub 2/ 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 H/sub 2/O/sub 2/ when H/sub 2/O/sub 2/ is generated at a rate comparable to that which leads to hemolysis in G6PD- deficient erythrocytes.},
doi = {},
url = {https://www.osti.gov/biblio/6402670}, journal = {Blood; (United States)},
number = ,
volume = 73:1,
place = {United States},
year = {Sun Jan 01 00:00:00 EST 1989},
month = {Sun Jan 01 00:00:00 EST 1989}
}