| Autor: |
Baker WL; Environment and Biotechnology Centre, Swinburne University of Technology, John Street, Hawthorn, 3122, Melbourne, Australia. wbaker@swin.edu.au, Key C, Lonergan GT |
| Jazyk: |
angličtina |
| Zdroj: |
Biotechnology progress [Biotechnol Prog] 2005 May-Jun; Vol. 21 (3), pp. 751-5. |
| DOI: |
10.1021/bp0500617 |
| Abstrakt: |
Beef liver catalases showed peroxidative activity using 2,2'-azino-bis-(3-ethylbenzthiazoline)-6-sulfonic acid as the electron donor and hydrogen peroxide as the acceptor at a pH of 5. This activity was not observed at pH 7. The reaction depended on acetate concentration, although succinate and propionate could partly replace the acetate as a catalyst. Other haem proteins also catalyzed a peroxidative effect. The reaction using syringaldazine or the coupling between dimethylaminobenzoic acid and 3-methyl-2-benzothiazolinone hydrazone was less effective and less sensitive. Evidence is presented that the reaction is associated with a conformational change of the catalase. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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