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Erythrocyte Superoxide Dismutase, Catalase and Glutathione Peroxidase in Glucose‐6‐Phosphate Dehydrogenase Deficiency
Author(s) -
Gerli Gian Carla,
Beretta Luciano,
Bianchi Maurizio,
Agostoni Angelo,
Gualandri Valter,
Orsini Giovan Battista
Publication year - 1982
Publication title -
scandinavian journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.904
H-Index - 84
eISSN - 1600-0609
pISSN - 0036-553X
DOI - 10.1111/j.1600-0609.1982.tb00574.x
Subject(s) - catalase , superoxide dismutase , glutathione peroxidase , glucose 6 phosphate dehydrogenase deficiency , glucose 6 phosphate dehydrogenase , antioxidant , peroxidase , biochemistry , enzyme , glutathione , chemistry , dehydrogenase , medicine , endocrinology , biology
Glucose‐6‐phosphate dehydrogenase (G‐6‐PD) deficient erythrocytes are particularly sensitive to oxidant stress. In order to evaluate if these cells are protected against oxidant damage, we assayed the antioxidant enzymes superoxide dismutase (SOD), catalase and glutathione peroxidase (GSH‐Px) in erythrocytes of G‐6‐PD deficient (hemizygous and heterozygous) subjects. Normal levels of antioxidant enzymes were found in all subjects examined both with positive and negative histories of haemolytic crisis after fava bean or drug ingestion. In contrast, high levels of catalase and GSH‐Px were found in a small group of G‐6‐PD deficient subjects (hemizygous and heterozygous) with β‐thalassaemia trait, probably by reason of the chronically enhanced oxidant stress which is present in β‐thalassaemia.