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.
Purification by dye-ligand chromatography of an NADP-dependent enzyme, 6-phosphogluconate dehydrogenase from lamb's liver
โ Scribed by A. Carne
- Publisher
- Elsevier Science
- Year
- 1982
- Tongue
- English
- Weight
- 249 KB
- Volume
- 121
- Category
- Article
- ISSN
- 0003-2697
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โฆ Synopsis
Purification of the NADP'-dependent 6-phosphogluconate dehydrogenase from lamb's liver using dye-ligand chromatography on Matrex Gel Red-A enabled a 2.5fold increase in yield of the enzyme and reduced the preparation time of a preivous scaled-up version of the published small-scale method.
๐ SIMILAR VOLUMES
2-Keto-3-deoxy-6-phosphogluconate aldolase (EC 4.1.2.14) has been isolated from extracts of Zymomonas mobilis using differential dye-ligand chromatography and affinity elution with product/product analog. The one-step procedure gives an enzyme with specific activity 600 units mg-1. Only 1 out of 47