form
solid
contains
≥10% water as stabilizer
mp
156 °C (dec.) (lit.)
SMILES string
NNc1ccc(cc1)[N+]([O-])=O
InChI
1S/C6H7N3O2/c7-8-5-1-3-6(4-2-5)9(10)11/h1-4,8H,7H2
InChI key
KMVPXBDOWDXXEN-UHFFFAOYSA-N
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
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
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
S R Carter et al.
Journal of inorganic biochemistry, 56(2), 127-141 (1994-11-01)
An improved purification scheme for an amine oxidase from equine plasma (EPAO), a nonruminant source, is described and the protein's active-site is characterized. EPAO is dimeric and contains one Type-2 Cu(II) ion per monomer. The EPAO Cu(II) site is spectroscopically