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Research Article| Volume 64, ISSUE 4, P601-612, October 1964

Hemolytic effect of primaquine. XVII. Hexokinase activity of glucose-6-phosphate dehydrogenase-deficient and normal erythrocytes

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      Abstract

      The activity of the sulfhydryl-dependent enzyme, hexokinase, was studied during hemolytic drug administration, in the erythrocytes of glucose-6-phosphate dehydrogenase deficient Negroes. The content of reduced glutathione in these erythrocytes is known to be low and to decrease further during primaquine-induced hemolytic anemia. The activity of hexokinase did not decrease in enzyme-deficient erythrocytes during the critical period from 2 to 5 days after the start of primaquine administration; this is the period during which the content of reduced glutathione has decreased but the hematocrit has not undergone its major fall, indicating that most of the erythrocytes damaged by drug are still in the circulation. The lack of any change in hexokinase activity during this period is evidence against irreversible inactivation of hexokinase resulting from depletion of reduced glutathione, and fails to implicate involvement of this enzyme in the mechanism of drug induced hemolysis. The activity of hexokinase in enzyme-deficient red cells prior to drug administration was significantly greater than that in normal erythrocytes. Further, during intense reticulocytosis following drug-induced hemolytic anemia or acute blood loss, the activity of hexokinase increased markedly. These findings are explained by a relationship between the age of the erythrocyte and its hexokinase activity. The existence of such a relationship was further confirmed by studies of the activity of hexokinase in relatively young and old erythrocytes separated by differential centrifugation. The decline in hexokinase activity as erythrocytes age may be of particular importance in the mechanism of red cell senescence.
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