Structural studies of penicillin acylase
โ Scribed by James A. Brannigan; Guy G. Dodson; Sarah H. Done; Lorraine Hewitt; Colin E. McVey; Keith S. Wilson
- Book ID
- 111635129
- Publisher
- Springer-Verlag
- Year
- 2000
- Tongue
- English
- Weight
- 218 KB
- Volume
- 88
- Category
- Article
- ISSN
- 0273-2289
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๐ SIMILAR VOLUMES
Penicillin acylase from Bacillus rneg~terj~lln was purified 5.22 fold using ultrafiltration followed bp ammonium sulphate precipitation and gel filtration chromatography using Sephades G-100. The final specific activity was 2.62 Uimg protein and was free from interfering proteases.
## Abstract Penicillin acylase has been immobilized to carboxymethylcellulose and to the resin Amberlite XAD7. The reaction kinetics of the enzyme were affected by both intrinsic (molecular) and microenvironmental effects. The Michaelis constant for the enzyme increased after immobilization as a re