Steroidumwandelnde Enzyme aus Mikroorganismen X. Anreicherung einer 4-En-3-oxosteroid-5α-Reduktase aus Mycobacterium smegmatis sowie Abtrennung und Anreicherung des Apoenzyms mit Hilfe der Affinitätschromatographie
✍ Scribed by Dr. P. Atrat; V. Deppmeyer; H. Groh; C. Hörhold
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 337 KB
- Volume
- 19
- Category
- Article
- ISSN
- 0233-111X
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✦ Synopsis
The 4-en-3-oxosteroid-5a-reductase from Mycobacterium smegmatis mas bound biospecifically on the affinant containing an immobilized testosterone ligand. The enzyme obtained by elution with ethylene glycol and urea in a 32 fold purity has a S. A. of 8.73 x p ~i androstenedione min-1 mg-'.
The coenzyme (FAD) could be separated from the immobilized enzyme substrate complex on the affinity matrix, in the presence of (NH,),SO, a t p H 3.0. After elution of the apoenzyme 979, of the initial enzyme activity was obtained by incubation with FAD. The reactivated enzyme results in a 40 fold enrichment.