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Key Documents

N1288

Sigma-Aldrich

NADH Oxidase from Bacillus licheniformis

lyophilized powder

Sinónimos:

NOX

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About This Item

Número de CAS:
9032-21-7
MDL number:
MFCD00164995
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Bacillus licheniformis

Quality Level

200

form

lyophilized powder

specific activity

≥35 units/mg protein

packaging

vial of ≥15 units

storage temp.

−20°C

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General description

NADH Oxidase is a surface enzyme with increased oxidative activity in polymorphonuclear leukocytes during phagocytosis.

Application

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 Actions

NADH Oxidase from Bacillus licheniformis was shown to display hydrogen peroxide-forming activity.

Unit Definition

One unit will oxidize 1.0 μmole NADH per minute at pH 7.0 at 30 °C.

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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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