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.
D001665:Binding Sites; D002021:Buffers; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D004912:Erythrocytes / Q000201:enzymology*; D005954:Glucosephosphate Dehydrogenase / Q000302:isolation & purification*; D006801:Humans; D009249:NADP / Q000032:analysis; D012685:Sepharose
D002021:Buffers; D009249:NADP; D012685:Sepharose; D005954:Glucosephosphate Dehydrogenase