Decomposition of hydrogen peroxide (H2O2) at physiological levels was studied in human
erythrocytes by means of a recently developed sensitive H2O2 assay. The exponential …

Genetic deficiencies of glucose-6-phosphate dehydrogenase (G6PD) and NADPH
predispose affected erythrocytes to destruction from peroxides. Conversely, genetic …

The catalase within normal, intact human erythrocytes was completely inactivated with
amino triazole. The rate of 14CO2 evolution, when the cells were subsequently incubated …

Purified enzymes were mixed to form a cell-free system that simulated the conditions for
removal of hydrogen peroxide within human erythrocytes. Human glutathione peroxidase …

Experiments were designed to evaluate the competition between erythrocyte catalase and
glutathione peroxidase for their common substrate, H202. When extracellular H2O2 …

To investigate the relative importance of catalase and glutathione in erythrocyte oxidant
defense, human and mouse (normal and acatalasemic) erythrocytes were reversibly lysed …

The contributions of catalase (H 2 O 2: H 2 O 2 oxidoreductase EC 1.11. 1.6) and glutathione
peroxidase (H 2 O 2: GSH oxidoreductase EC 1.11. 1.19) to the removal of H 2 O 2 from red …

Mammalian erythrocytes have large amounts of catalase, an enzyme which catabolizes
hydrogen peroxide (H2O2). Because catalase has a low affinity for H2O2, others have …

Red blood cells are frequently employed in studies of oxidative stress. Technical difficulties
have previously prevented the measurement of H 2 O 2 production by red blood cells …

Catalase and glutathione peroxidase (GSHPX) react with red cell hydrogen peroxide. A
number of recent studies indicate that catalase is the primary enzyme responsible for …