Blood, 1970, Vol. 35, No. 2, pp. 166-172.
© 1970 American Society of Hematology, Inc.
Reduction of Oxidized Glutathione in Normal and
Glucose-6-Phosphate Dehydrogenase Deficient
Erythrocytes and Their Hemolysates
EGMOND E. RIEBER 1 and
ERNST R. JAFFÉ 1
1 Department of Medicine, Albert Einstein College of Medicine-Bronx Municipal
Hospital Center and Lincoln Hospital, Bronx, N. Y.
When assayed by the ability to reduce oxidized glutathione to reduced
glutathione, glucose-6-phosphate dehydrogenase deficiency of either the Negro
or Caucasian mutant variety could be demonstrated in hemolysates only with
hemoglobin concentrations below 2.0 Gm. per 100 ml. In intact erythrocytes, the
inability to regenerate reduced glutathione was apparent regardless of the concentration of red cells. The process of hemolysis, therefore, appeared to permit
the demonstration of higher levels of activity in G-6-PD deficient human erythrocytes than was possible in intact cells. A markedly deficient capacity to
regenerate endogenous reduced glutathione or to reduce exogenous oxidized
glutathione, however, could be demonstrated with the hemolysate of erythrocytes from a patient with hereditary nonspherocytic hemolytic anemia associated with a deficiency of glucose-6-phosphate dehydrogenase activity. These
studies have emphasized the hazards involved in extrapolating the results of
studies performed with hemolysates to metabolic processes within intact
erythrocytes.
Submitted on August 11, 1969
Accepted on October 10, 1969
