## Abstract Nitrile hydratase from __Brevibacterium__ sp. R312 was purified to homogeneity. The isoelectric point was 5.75. The two kinds of subunits were separated by reverse phase HPLC and their Nβterminal amino acid sequences were found to be identical to those of __Rhodococcus__ sp. Nβ774 nitri
β¦ LIBER β¦
N-terminal amino acid sequence ofBrevibacteriumsp. R312 wide-spectrum amidase
β Scribed by Chan K. N. Chan Kwo Chion; Robert Duran; Alain Arnaud; Pierre Galzy
- Publisher
- Springer
- Year
- 1991
- Tongue
- English
- Weight
- 388 KB
- Volume
- 36
- Category
- Article
- ISSN
- 1432-0614
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β¦ Synopsis
A wide-spectrum amidase from Brevibacterium sp. R312 was partially purified. The enzyme subunit was purified by reversed phase HPLC and the N-terminal amino acid sequence was found to be identical to that of Pseudomonas aeruginosa aliphatic amidase.
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