Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes
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.
- Research Organization:
- Univ. of Genoa (Italy)
- OSTI ID:
- 6402670
- Journal Information:
- Blood; (United States), Vol. 73:1
- Country of Publication:
- United States
- Language:
- English
Similar Records
Ozone interaction with rodent lung: effect on sulfhydryls and sulfhydryl-containing enzyme activities
Leflunomide attenuates oxidative stress in fetal human lung endothelial cells via superoxide dismutase 2 and catalase
Related Subjects
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