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Favism: a hemolytic disease associated with increased superoxide dismutase and decreased glutathione peroxidase activities in red blood cells

Mavelli, Irene and Ciriolo, Maria Rosa and Rossi, Luisa and Meloni, Tullio and Forteleoni, Gavino and De Flora, Antonio and Benatti, Umberto and Morelli, Alessandro and Rotilo, Giuseppe (1984) Favism: a hemolytic disease associated with increased superoxide dismutase and decreased glutathione peroxidase activities in red blood cells. European Journal of Biochemistry, Vol. 139 (1), p. 13-18. eISSN 1432-1033. Article.

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DOI: 10.1111/j.1432-1033.1984.tb07969.x

Abstract

Red blood cells of favism patients with acute hemolytic crisis have markedly more superoxide dismutase (superoxide: superoxide oxidoreductase, EC 1.15.1.1) and less glutathione peroxidase (glutathione: hydrogen-peroxide oxidoreductase, EC 1.11.1.9) than either normal controls, glucose-6-phosphate dehydrogenase-deficient subjects or favism patients outside hemolytic crisis. This altered value of the two enzyme activities is not due to increased reticulocyte content of blood. The electrophoretic triplet pattern of superoxide dismutase is also changed, with significant increase of the most positively charged band. Similar modifications of the two enzyme activities are observed after treatment of normal red blood cells with high concentrations of divicine and ascorbate, which are redox compounds that are contained in fava seeds. This treatment produces no hemolysis, but leads to hemolysis if the treated cells are resuspended in the homologous plasma. These results suggest a possible role of active oxygen species in the development of favism.

Item Type:Article
ID Code:1268
Status:Published
Refereed:Yes
Uncontrolled Keywords:Favism, superoxide dismutase, glutathione peroxidase, red blood cells
Subjects:Area 06 - Scienze mediche > MED/38 Pediatria generale e specialistica
Divisions:001 Università di Sassari > 01 Dipartimenti > Neuroscienze, scienze materno infantili
Publisher:Blackwell Science on behalf of the Federation of European Biochemical Societies / Wiley
eISSN:1432-1033
Copyright Holders:© FEBS 1984
Deposited On:18 Aug 2009 10:04

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