Inactivation of glutathione peroxidase following hemoglobin oxidation.
Inactivation of erythrocyte GSH-peroxidase correlates with the rate of hemoglobin oxidation. The presence of superoxide dismutase and catalase only marginally reduces the rate of inactivation of the enzyme indicating that the loss of activity is not due to oxygen radicals produced during oxidation of hemoglobin. The inactivation of glutathione peroxidase is due by-and-large to the formation of hemichromes.
Grelloni
F
F
Department of Molec., Cell. and Animal Biology, University of Camerino, Italy.
Gabbianelli
R
R
Falcioni
G
G
D000818:Animals; D002374:Catalase / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D004912:Erythrocytes / Q000201:enzymology; D005979:Glutathione Peroxidase / Q000037:antagonists & inhibitors*; D006420:Hemeproteins / Q000494:pharmacology*; D006454:Hemoglobins / Q000378:metabolism*; D010084:Oxidation-Reduction; D013482:Superoxide Dismutase / Q000494:pharmacology; D014337:Trout / Q000097:blood
D006420:Hemeproteins; D006454:Hemoglobins; C001332:hemichrome; D002374:Catalase; D005979:Glutathione Peroxidase; D013482:Superoxide Dismutase