Rapid purification of human erythrocyte 6-phosphogluconate dehydrogenase by means of affinity chromatography.

A rapid two-step procedure is reported by which homogeneous 6-Phosphogluconate dehydrogenase can be isolated from human erythrocytes. This method is based upon direct affinity chromatography of the hemolysates on adenosine 2',5'-bisphosphate-agarose (yielding a 4,500-fold purification), followed by anion exchange chromatography on a micro-column of DEAE-Sephadex. The present method represents a considerable simplification over previously available procedures for the purification of this enzyme protein from human erythrocytes.