InChI key
KMVPXBDOWDXXEN-UHFFFAOYSA-N
InChI
1S/C6H7N3O2/c7-8-5-1-3-6(4-2-5)9(10)11/h1-4,8H,7H2
SMILES string
NNc1ccc(cc1)[N+]([O-])=O
form
solid
contains
≥10% water as stabilizer
mp
156 °C (dec.) (lit.)
signalword
Danger
Hazard Classifications
Acute Tox. 4 Dermal - Acute Tox. 4 Oral - Expl. 1.1 - Eye Irrit. 2 - Flam. Sol. 2 - Skin Irrit. 2 - Skin Sens. 1 - STOT SE 3
target_organs
Respiratory system
存储类别
1 - Explosive hazardous materials
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
V Steinebach et al.
Analytical biochemistry, 230(1), 159-166 (1995-09-01)
Pig kidney diamine oxidase was purified to homogeneity. The reaction product of the cofactor with p-nitrophenylhydrazine (pNPH) was liberated with pronase treatment and purified. 1H NMR, uv/vis, and electrospray tandem mass spectroscopy revealed it to be a dipeptide with the
I Frébort et al.
European journal of biochemistry, 225(3), 959-965 (1994-11-01)
Interactions of two distinct quinoprotein amine oxidases from Aspergillus niger, AO-I and AO-II, with active-site covalent modifiers have been investigated. Both enzymes are inhibited similarly by phenylhydrazine or p-nitrophenylhydrazine, forming an orange Schiff base with a carbonyl group of topaquinone
Analytical and mechanistic aspects of the electrochemical oxidation of keto steroids derivatized with phenylhydrazine, (4-nitrophenyl)hydrazine, and (2,4-dinitrophenyl)hydrazine.
A M Bond et al.
Analytical chemistry, 60(10), 1023-1027 (1988-05-15)
I Frébort et al.
Biochemistry and molecular biology international, 36(6), 1207-1216 (1995-08-01)
Structural properties of dimeric (2 x 75 kDa) copper-containing amine oxidase (EC 1.4.3.6) from Aspergillus niger were studied. The enzyme treated with SDS was dissociated into subunits which showed different mobility on polyacrylamide gel without SDS. The separated subunits had
Atsuko Satoh et al.
Biochimica et biophysica acta, 1647(1-2), 272-277 (2003-04-11)
Quinohemoprotein amine dehydrogenase (QH-AmDH) catalyzes the oxidative deamination of aliphatic and aromatic amines. The enzyme from Pseudomonas putida has an alpha beta gamma heterotrimeric structure with two heme c groups in the largest alpha subunit, and a novel quinone cofactor
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