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Purification and preliminary characterization of alcohol dehydrogenase from Aspergillus nidulans.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Creaser, Ernest H. Porter, Robert L. Britt, Katrina Pateman, J. A. J. Doy, Colin H. |
| Copyright Year | 1985 |
| Abstract | Aspergillus alcohol dehydrogenase is produced in response to growth in the presence of a wide variety of inducers, of which the most effective are short-chain alcohols and ketones, e.g. butan-2-one and propan-2-ol. The enzyme can be readily extracted from fresh or freeze-dried cells and purified to homogeneity on Blue Sepharose in a single step by using specific elution with NAD+ and pyrazole. The pure enzyme has Mr 290 000 by electrophoresis or gel filtration; it is a homopolymer with subunit Mr 37 500 by electrophoresis in sodium dodecyl sulphate; its amino acid composition corresponds to Mr 37 900, and the native enzyme contains one zinc atom per subunit. The enzyme is NAD-specific and has a wide substrate activity in the forward and reverse reactions; its activity profile is not identical with those of other alcohol dehydrogenases. |
| File Format | PDF HTM / HTML |
| DOI | 10.1042/bj2250449 |
| PubMed reference number | 3156582 |
| Journal | Medline |
| Volume Number | 225 |
| Issue Number | 2 |
| Alternate Webpage(s) | http://www.biochemj.org/content/ppbiochemj/225/2/449.full.pdf |
| Alternate Webpage(s) | https://doi.org/10.1042/bj2250449 |
| Journal | The Biochemical journal |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
