## Abstract Das konventionelle Reinigungsverfahren von Glucose‐6‐phosphat‐dehydrogenase (G6PDH) (E.C. 1.1.1.49) aus Rinder‐Nebennierenrinde wird durch eine einzige affinitätschromatographische Trennungsstufe ersetzt. Die Anwendung einer mit Nicotinamid‐Adenin‐Dinukleotid‐Phosphat (NADP) substituier
The purification of yeast glucose 6-phosphate dehydrogenase by dye-ligand chromatography
✍ Scribed by Edward E. Farmer; John S. Easterby
- Publisher
- Elsevier Science
- Year
- 1984
- Tongue
- English
- Weight
- 280 KB
- Volume
- 141
- Category
- Article
- ISSN
- 0003-2697
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✦ Synopsis
Glucose 6-phosphate dehydrogenase (EC 1.1.1.39) has been purified to homogeneity from baker's yeast by a simple procedure involving affinity elution from a column of red triazine dye, H-8BN, immobilized to Sepharose 6B. Eight milligrams of homogeneous protein is obtained in 53% yield from 200 g of dried yeast. This represents the first published purification of the enzyme from Saccharomyces Cerevisiae.
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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.
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