Altered Electrophoretic Mobility of the Human Erythrocytic Glucose-6-phosphate Dehydrogenase as a Function of their in vivo Ages

Abstract

Human red cells were separated, by centrifugation by virtue of their density gradient due to lipid contents, into the younger and older cells. Lipid analysis confirmed that the older red cells have lower content than their younger conterparts. Crude G6PD's derived from each younger and older red cells were subjected to cellulose acetate electrophoresis, and their activities were assayed spectrophotometrically. The activity declined apparently as aging takes place, with little or no changes in their glutathione contents. Formazan bands on electropherograms of both G6PD's derived from both cells clearly disclosed the fact that the G6PD from the older cell migrates roughly 1.2 times faster toward anode than the enzyme from the younger cell. The alteration of the G6PD mobility as well as its activity was more accentuated with additon of 2-mercaptoethanol and cysteine.