Purification of human red cell glucose 6-phosphate dehydrogenase by affinity chromatography.

Human glucose 6-phosphate dehydrogenase associated with NADPH was efficiently bound with agarose-bound NADP, whereas the enzyme associated with NADP was poorly bound with agarose-bound NADP. After the elimination of haemoglobin from haemolyzate by treatment with DEAE-cellulose, the enzyme was converted into the NADPH-bound form and was applied on an affinity column. The enzyme was specifically eluted from the column by NADP in the elution buffer. A homogeneous enzyme preparation was obtained in high yield.