Isoelectric focusing of hexokinase and glucose-6-phosphate dehydrogenase isoenzymes in erythrocytes of newborn infants and adults.

Isoenzymes of glucose-6-phosphate dehydrogenase and hexokinase from red cells of newborn infants were analysed by isoelectric focusing in polyacrylamide gel after partial purification. The pattern of isoenzyme distribution was compared with that of erythrocytes from adults. Glucose-6-phosphate dehydrogenase isoenzyme distribution was identical between erythrocytes from newborn infants and adults. Erythrocytic hexokinase isoenzymes patterns were different between newborn infants and adults. Erythrocytes from adults contain a hexokinase isoenzyme which has the same isoelectric point as rat liver hexokinase isoenzyme I (pH 6 . 01). This isoenzyme is lacking in red cells from newborn infants. Isoenzymes with the isoelectric properties of rat liver isoenzyme II (pH 5 . 48) were not detectable in red cells from adults, nor from newborn infants. The occurrence of an isoenzyme III in red cells remained unclear, because only a faint staining was observed in the corresponding region of erythrocytic gels. Preliminary results revealed a fetal type of hexokinase isoenzyme distribution in infants with an age of 10 months. This indicates that regulation of the synthesis of Hb F and of fetal hexokinase isoenzymes is not correlated.