Abstract
A method for the assay of red cell galactokinase is presented. Commercially available 14C-galactose is purified by incubating with ATP, magnesium, and hexokinase and passed through a small DEAE column. Hemolysate is mixed with a reaction mixture, incubated, and the 14C-galactose which has been phosphorylated is trapped on DEAE paper. The reactivity of unlabeled galactose solutions was found to change for a considerable period of time, not only because of mutarotation, but also because of the formation of a keto sugar. Glucose was found to exert a stabilizing effect on the enzyme when stored in intact cells. The enzyme activity of the red cells of children aged 4–16 were not found to be significantly higher than those of adults. Galactose intake did not appear to influence the level of the enzyme in red cells, but blood samples containing a high percentage of reticulocytes tended to have somewhat higher levels of enzyme than the blood of normal subjects.
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