N1288
NADH Oxidase from Bacillus licheniformis
lyophilized powder
Synonym(e):
NOX
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About This Item
Empfohlene Produkte
Biologische Quelle
Bacillus licheniformis
Qualitätsniveau
Form
lyophilized powder
Spezifische Aktivität
≥35 units/mg protein
Verpackung
vial of ≥15 units
Lagertemp.
−20°C
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Allgemeine Beschreibung
NADH Oxidase is a surface enzyme with increased oxidative activity in polymorphonuclear leukocytes during phagocytosis.
Anwendung
NADH Oxidase from Bacillus licheniformis has been used in a study to assess nitrogen assimilation by Bacillus licheniformis growing in chemostat cultures. It has also been used in a study to investigate the role of glutamate dehydrogenase in ammonia assimilation in Bacillus macerans.
Biochem./physiol. Wirkung
NADH Oxidase from Bacillus licheniformis was shown to display hydrogen peroxide-forming activity.
Einheitendefinition
One unit will oxidize 1.0 μmole NADH per minute at pH 7.0 at 30 °C.
Signalwort
Danger
H-Sätze
P-Sätze
Gefahreneinstufungen
Resp. Sens. 1
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 1
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
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Nitrogen Assimilation by Bacillus licheniformis Organisms Growing in Chemostat Cultures
Meers, J. and L. Pederson
Microbiology, 70, 277-286 (1972)
Y Nishiyama et al.
Journal of bacteriology, 183(8), 2431-2438 (2001-03-29)
Amphibacillus xylanus and Sporolactobacillus inulinus NADH oxidases belonging to the peroxiredoxin oxidoreductase family show extremely high peroxide reductase activity for hydrogen peroxide and alkyl hydroperoxides in the presence of the small disulfide redox protein, AhpC (peroxiredoxin). In order to investigate
R T Briggs et al.
The Journal of cell biology, 67(3), 566-586 (1975-12-01)
The ultrastructural localization of NADH oxidase, a possible enzyme in the increased oxidative activity of polymorphonuclear leukocytes (PMN) during phagocytosis, was studied. A new cytochemical technique for the localization of H2O2, a product of NADH oxidase activity, was developed. Cerous
K Kanamori et al.
Journal of bacteriology, 169(10), 4692-4695 (1987-10-01)
Pathways of ammonia assimilation into glutamic acid in Bacillus macerans were investigated by measurements of the specific activities of glutamate dehydrogenase (GDH), glutamine synthetase, and glutamate synthase. In ammonia-rich medium, GDH was the predominant pathway of ammonia assimilation. In nitrogen-fixing
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