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

  • 1 July 1979
    • journal article
    • Vol. 28  (4) , 280-4
Abstract
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.

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