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Merck
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主要文件

N1288

Sigma-Aldrich

NADH Oxidase from Bacillus licheniformis

lyophilized powder

别名:

NOX

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About This Item

CAS号:
MDL號碼:
分類程式碼代碼:
12352204
NACRES:
NA.54

生物源

Bacillus licheniformis

品質等級

形狀

lyophilized powder

比活性

≥35 units/mg protein

包裝

vial of ≥15 units

儲存溫度

−20°C

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一般說明

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

應用

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.

單位定義

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

象形圖

Health hazard

訊號詞

Danger

危險聲明

防範說明

危險分類

Resp. Sens. 1

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves, type N95 (US)


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)
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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