A spectrophotometric method for kinetic studies with quinone-dependent oxidoreductases. Application to detection in membranes of nitrate reductase activity with menadione and duroquinone as electron donors
In: Enzyme and microbial technology, Jg. 22 (1998), Heft 3, S. 165-169
academicJournal
- print, 12 ref
Zugriff:
A simple method for estimating the activity of membrane-bound quinone-dependant oxidoreductases is described. Nitrate reductase from membranes of Escherichia coli is used as a model with menadione and duroquinone, commercially available analogues of the physiological substrates, menaquinone and ubiquinone, as electron donors. These analogues are reduced by KBH4 (which is specific for aldehydes and ketones) using molar ratios of [KBH4]/[MENADIONE] = 20 and [KBH]/[duroquinone] = 10. The appearance of the oxidized state can be monitored with a classical spectrophotometer and does not require a dual wavelenght or diffusing-medium apparatus. To avoid turbidity in the cuvette, small amounts of membrane containing overexpressed enzyme are used.
Titel: |
A spectrophotometric method for kinetic studies with quinone-dependent oxidoreductases. Application to detection in membranes of nitrate reductase activity with menadione and duroquinone as electron donors
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Autor/in / Beteiligte Person: | BUC, J ; GIORDANI, R |
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Zeitschrift: | Enzyme and microbial technology, Jg. 22 (1998), Heft 3, S. 165-169 |
Veröffentlichung: | Amsterdam: Elsevier Science, 1998 |
Medientyp: | academicJournal |
Umfang: | print, 12 ref |
ISSN: | 0141-0229 (print) |
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