Abstract
Abstract
Normal erythrocytes incubated with inosine and adenine in an acid citrate/dextrose medium underwent a marked, but reversible, loss of glutathione reductase activity reflected by erythrocyte glutathione reductase activity coefficients in the range 3.21 ± 0.39. The system therefore appears to simulate riboflavin deficiency in isolated red cells as assessed by this index. Deactivation was dependent on cell metabolism and was inhibited by treatment with methylene blue, ascorbate, and fluoride or by low temperature. The rate of deactivation was greatly increased by lowering the pH and by the presence of phosphate ions.
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