Overproduction and characterization of a recombinantD-amino acid oxidase fromArthrobacter protophormiae
β Scribed by Birgit Geueke; Andrea Weckbecker; Werner Hummel
- Publisher
- Springer
- Year
- 2007
- Tongue
- English
- Weight
- 450 KB
- Volume
- 74
- Category
- Article
- ISSN
- 1432-0614
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An L-amino-acid oxidase (EC 1.4.3.1) that catalyzes the oxidative deamination of twelve L-amino acids has been purified 21-fold and with 14% yield to electrophoretic homogeneity from Chlamydomonas reinhardtii cells by ammonium-sulfate fractionation, gel filtration through Sephacryl and Superose, ani
Neurospora crassa possesses an inducible L-amino acid oxidase that is expressed only when cells are derepressed for nitrogen in the presence of an amino acid. Enzyme synthesis requires both induction by an amino acid and simultaneous nitrogen catabolite derepression. Carbon limition in the presence