Abstract
Glucose 6-phosphate dehydrogenases extracted from various organs of mice, rats, hamsters and guinea pigs, and from human red blood cells were separated into several molecular forms by means of acrylamide disc electrophoresis.
Two major forms of G6PD were demonstrated in each animal which differed not only in electrophoretic mobility, but also in intracellular location and reactivity to inhibitors; one moved slowly, located mainly in microsomal fraction and was resistant to inhibitors, while the other moved rapidly, located in mitochondria and cell sap, and was sensitive to inhibitors. The latter form of G6PD appeared to be homologous to the sex-linked G6PD of human red cells.
Isoenzyme pattern showed sex difference in the liver of rats and in the plasma of mice. In the rat liver, band D enzyme was more active in females than in males, while in mouse plasma, band I enzyme was more active in males than in females. Both bands exhibited the same electrophoretic mobility.
