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安全信息

N1288

Sigma-Aldrich

NADH Oxidase from Bacillus licheniformis

lyophilized powder

别名:

NOX

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About This Item

CAS号:
MDL编号:
UNSPSC代码:
12352204
NACRES:
NA.54

生物来源

Bacillus licheniformis

质量水平

表单

lyophilized powder

比活

≥35 units/mg protein

包装

vial of ≥15 units

储存温度

−20°C

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一般描述

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

应用

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.

生化/生理作用

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

单位定义

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

象形图

Health hazard

警示用语:

Danger

危险声明

预防措施声明

危险分类

Resp. Sens. 1

储存分类代码

11 - Combustible Solids

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)

法规信息

常规特殊物品

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Nitrogen Assimilation by Bacillus licheniformis Organisms Growing in Chemostat Cultures
Meers, J. and L. Pederson
Microbiology, 70, 277-286 (1972)
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
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
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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