Abstract
Human 6-phosphogluconate dehydrogenase (6PGD) was purified from hemolyzate by group affinity chromatography on 2',5'-ADP-Sepharose, followed by buffer exchange chromatography on Sephadex G-25 and finally salting-out chromatography on Sepharose 6B. An apparatus was assembled from commercially available elements, in which the purification procedure can proceed and be completed unattended and under fully automatic control. The weekly production of the set-up is at present 10 mg of pure 6PGD. The choice of the purification of procedure and the advantages of automation are discussed.
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