A further characterization of alanine dehydrogenase from Streptomyces aureofaciens
✍ Scribed by Ivana Vančurová; Aleš Vančura; Jindřich Volc; Jiří Neužil; Vladislav Běhal
- Publisher
- John Wiley and Sons
- Year
- 1989
- Tongue
- English
- Weight
- 283 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0233-111X
No coin nor oath required. For personal study only.
✦ Synopsis
A further characterization of alanine dehydrogenase from Streptomyces aureofaciens
📜 SIMILAR VOLUMES
Two enzymes, amylase and protease of Streptomyces species were purified by a combination of ion exchange chromatography and gel filtration and characterized. The amylase had an exoaction on starch yielding maltose as a major end product and was identified as beta-amylase. The purified amylase had a
A 20 kDa antifungal serine protease from Streptomyces sp. A6 was purified to 34.56 folds by gel permeation chromatography. The enzyme exhibited highest activity at neutral to near alka- line pH 7-9 and 55 °C. Neutral surfactant triton X-100 enhanced the activity by 4.12 fold. The protease activity a
## Abstract The neutral metalloprotease extracted from 1,200 gm of human articular cartilage was purified 1,400‐ to 2,400‐fold by diethylaminoethyl‐ and carboxymethyl‐Sephadex chromatography. Disc electrophoresis and an isoelectric focusing method resolved the neutral enzyme activity into 4 bands.