Abstract
Extract: Electrophoretic properties of glucose-6-phosphate dehydrogenase (G6PD) were studied in mother-infant pairs and in young and old erythrocytes of adults. G6PD isoenzymes of erythrocytes of newborn infants migrated at rates 3–4% faster than the corresponding isoenzymes of maternal erythrocytes. Analysis of hemolysates of young and old erythrocytes of adults revealed that G6PD of young cells also moved about 3% faster than that of old cells. In contrast, active enzyme sedimentation analysis revealed that the G6PD enzyme proteins of old and young erythrocytes of adults, of newborns, and of their mothers sedimented with essentially identical rates (S20,w = 6.8). Migration in gels of different acrylamide concentrations and velocity sedimentation analysis indicated that the G6PD of old and of young erythrocytes was in the same state of aggregation. Extensive equilibration of the hemolysates with nicotinamide-adenine dinucleotide phosphate (NADP) by filtration through Sephadex G-25 induced a clear increase in the migration rate of the G6PD of old cells of adults and of mothers at term to the rate characteristic of the enzyme of neonates and of young cells of adults. Experiments in which NADP was labeled with 14C indicated that, in the process of gel nitration, the NADP content of the aged G6PD was restored. Thus the rate of migration of G6PD in acrylamide gel seems to be a function of the amount of NADP bound.
Similar content being viewed by others
Article PDF
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Bakay, B., Nyhan, W. & Monkus, E. Change in Electrophoretic Mobility of Glucose-6-Phosphate Dehydrogenase with Aging of Erythrocytes. Pediatr Res 6, 705–712 (1972). https://doi.org/10.1203/00006450-197207000-00003
Issue Date:
DOI: https://doi.org/10.1203/00006450-197207000-00003