D7876
二胺氧化酶 来源于猪肾脏
≥0.05 unit/mg solid
别名:
胺：氧氧化还原酶（脱氨）（含吡哆醛）
产品名称
二胺氧化酶 来源于猪肾脏, ≥0.05 unit/mg solid
biological source
Porcine kidney
form
solid
specific activity
≥0.05 unit/mg solid
mol wt
170 kDa
solubility
100 mM sodium phosphate buffer, pH 7.2: soluble 10 mg/mL
foreign activity
monoamine oxidase (benzylamine substrate) ≤1%
storage temp.
−20°C
Quality Level
Application
来自猪肾的二胺氧化酶已被用于研究测定鸟氨酸脱羧酶活性的基于发光的测试。来自猪肾的二胺氧化酶也用于研究二胺氧化酶中 N-连接寡糖结构。
猪肾来源的二胺氧化酶已用于制备组胺生物传感器。
Biochem/physiol Actions
二胺氧化酶催化单胺、二胺和组胺氧化成为醛、氨和过氧化氢。该酶属于含铜的胺氧化酶，是氮代谢中的关键酶。二胺氧化酶受到二乙基二硫代氨基甲酸、苯肼、氨基脲、氰化物、异烟酸肼抑制。
General description
猪肾来源的二胺氧化酶是由两个分子量均为87kDa的相同亚基组成的同二聚体，每个亚基含有一个吡哆醛磷酸分子和一个铜原子。酶分子量为170kDa。酶是一种糖蛋白，含有5%己糖、3.3%葡萄糖胺、2.6% N-乙酰葡萄糖胺和0.25% N-乙酰神经氨酸。酶对刀豆蛋白A具有高亲和力。以尸胺和组胺作为底物时的最适pH为6.3-7.4。
Other Notes
在 pH 7.2 和 37℃ 条件下，1 个单位每小时将氧化 1.0 μmol 腐胺。
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
低风险生物材料
动植物源性产品
此项目有
Marta Moniente et al.
Food research international (Ottawa, Ont.), 160, 111735-111735 (2022-09-10)
Lentilactobacillus parabuchneri is the main bacteria responsible for the accumulation of histamine in cheese. The goal of this study was to assess the efficiency of potential histamine-degrading microbial strains or, alternatively, the action of the diamine oxidase (DAO) enzyme in
M A Shah et al.
The Biochemical journal, 253(1), 103-107 (1988-07-01)
Pig kidney diamine oxidase (DAO) was found to contain 5% (w/w) natural hexose, 3.25% glucosamine, 2.61% N-acetylglucosamine and 0.25% N-acetylneuraminic acid. The enzyme exhibited strong affinity towards concanavalin A (Con A) with a stoichiometry of 1:4.6. The kinetics of interaction
A PRELIMINARY INVESTIGATION ON A HISTAMINE BIOSENSOR CONSTRUCTED FROM DIAMINE OXIDASE IMMOBILISED ONTO AN OXYGEN PROBE
Gupta N MM, et al.
International Journal of Pharmaceutical Sciences and Research (2018)
Y Huang et al.
Carbohydrate research, 323(1-4), 111-125 (2000-04-27)
Structures of the N-linked glycans released from porcine kidney diamine oxidase (DAO) were characterized utilizing various analytical techniques, including matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI/TOF-MS), high-performance capillary electrophoresis (HPCE), and high-pH anion-exchange chromatography with pulsed amperometric detection (HPAEC-PAD). The
A Rinaldi et al.
Preparative biochemistry, 12(1), 11-28 (1982-01-01)
Several methods for the isolation of apparently homogeneous pig kidney diamine oxidase have been reported in recent years (1-7), but these procedures allow to obtain only little amounts of material making very difficult the study of the molecular properties of
实验方案
To standardize a procedure for the enzymatic assay of Diamine Oxidase.
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