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Mediterranean glucose 6‐phosphate dehydrogenase (G6PD) deficiency – Near normal decay of the mutant enzyme protein in circulating erythrocytes
Author(s) -
Morelli Alessandro,
Benatti Umberto,
Guida Lucrezia,
Flora Antonio
Publication year - 1984
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.1600-0609.1984.tb02389.x
Subject(s) - dehydrogenase , mutant , intracellular , glucose 6 phosphate dehydrogenase , enzyme , biochemistry , glucosephosphate dehydrogenase deficiency , platelet , enzyme assay , biology , mutant protein , oxidative stress , chemistry , oxidative phosphorylation , immunology , gene
Complete removal of leucocytes and platelets from erythrocytes and the development of a sensitized procedure for the assay of G6PD activity allowed the biochemical mechanisms of the Mediterranean variety of G6PD deficiency to be re‐evaluated. Activity in the young erythrocytes from 9 G6PD‐deficient subjects averaged 0.1% of the levels observed in the corresponding erythrocyte fraction from normal individuals: moreover, the decline of activity during aging of the G6PD‐deficient erythrocytes was comparable with that observed for the normal enzyme. Mutant G6PD purified from granulocytes of a G6PD‐deficient subject and entrapped within the corresponding erythrocytes was remarkably stable. Exposure of native erythrocytes to an oxidative stress (divicine plus ascorbate) resulted in a decrease of G6PD activity that was significantly more rapid and extensive in control than in G6PD‐deficient cells. These results seem to exclude enhanced intracellular breakdown of the mutant protein within the circulating erythrocytes.