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Issue Date
1992Submitted date
2024-04-17
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Show full item recordAbstract
A NADHoxidase from Thermus thermophilus HB8 was purified to homogeneity by a procedure that is easy to scale up. The hydrogen peroxide forming NADH oxidase was found to be a monomerof 26 kD by SDSPAGE, oxidation of NADH (NADPH) occuredin the presence of O, and either FMN or FAD. These cofactors also enhancedthe stability of the enzyme towards higher temperatures and extreme pH. The properties of the NADH oxidase are discussed in respectofits applicability in biosensor techniques.Citation
Biosensors : fundamentals, technologies and applications, 245 - 250Affiliation
GBF, Gesellschaft fur Biotechnologische Forschung mbH, Mascheroder Weg1, W-3300 Braunschweig, F.R.G.; Laboratorium für Biochemie, Universität Bayreuth, Universitätsstr. 30, W-8580 Bayreuth, F. R. G.Type
Book chapterconference paper
Language
enSeries/Report no.
GBF monographs ; Volume 17ISSN
0930-4320ISBN
35272843701560812206
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