Use of differential dye-ligand chromatography with affinity elution for enzyme purification: 6-Phosphogluconate dehydratase from Zymomonas mobilis

✍ Scribed by R.K. Scopes; K. Griffiths-Smith

• Publisher: Elsevier Science
• Year: 1984
• Tongue: English
• Weight: 404 KB
• Volume: 136
• Category: Article
• ISSN: 0003-2697
• DOI: 10.1016/0003-2697(84)90257-4

✦ Synopsis

Using differential dye-ligand chromatography and affinity elution with a substrate analog, 6-phosphogluconate dehydratase (EC 4.2.1.12) has been isolated from extracts of Zymomonas mobilis in a one-step procedure with 50% recovery. The specific activity of freshly isolated enzyme was 245 units mg-1. The enzyme contains iron, and it is rapidly inactivated in oxidizing conditions. It is inhibited by glycerophosphates, most strongly by the D-alpha-isomer which structurally corresponds to half of the substrate molecule.