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Effect of Oxidized Glutathione and Acetylphenylhydrazine on Haemoglobin from Normal and Glucose‐6‐Phosphate Dehydrogenase Deficient Individuals
Author(s) -
Zaidman Jacob
Publication year - 1970
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1970.tb01619.x
Subject(s) - incubation , chemistry , glutathione , glucose 6 phosphate dehydrogenase , dehydrogenase , biochemistry , chromatography , enzyme
S ummary After incubation of haemolysates of normal and G6PD‐deficient red cells with oxidized glutathione, the GSSG is differently bound to the various HbA 3 minor components (as demonstrated by Amberlite CG‐50 column chromatography) of the two kinds of red cells. In normal haemolysates the interaction is with the HbA 3e component, and in G6PD‐deficient haemolysates with the HbA 3d and HbA 3e components. After incubation of normal and G6PD‐deficient red cells with acetylphenylhydrazine, in the presence of glucose, where GSH is oxidized to GSSG, interaction is observed only in the enzyme‐deficient red cells with the same components as observed in the incubation with GSSG.