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 d
Separate detection of glucose-6-phosphate dehydrogenase from 6-phosphogluconate dehydrogenase by DEAE-paper chromatography
✍ Scribed by Misumi, Hiromasa ;Wada, Hiroshi ;Ichiba, Yozo ;Shohmori, Toshikiyo ;Kosaka, Mutsutoshi
- Publisher
- Springer-Verlag
- Year
- 1982
- Weight
- 721 KB
- Volume
- 45
- Category
- Article
- ISSN
- 1432-0584
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## 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
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.
The isolation of glucose-6-phosphate dehydrogenase from outdated human erythrocytes (type AB+) utilizing NADP+ affinity chromatography and gel-permeation chromatography (Bio-Gel P-150) yields a fully active, homogeneous preparation. The procedure is faster and gives a higher yield than previous repo