质量水平
方案
97%
沸点
90-92 °C/1 mmHg (lit.)
mp
41-44 °C (lit.)
储存温度
2-8°C
SMILES字符串
NNc1ccccn1
InChI
1S/C5H7N3/c6-8-5-3-1-2-4-7-5/h1-4H,6H2,(H,7,8)
InChI key
NWELCUKYUCBVKK-UHFFFAOYSA-N
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应用
- 增强金属去除功能：利用由2-肼吡啶衍生的希夫碱功能化双醛淀粉，在增强溶液中Cu(II)的去除方面显示出显著的潜力。该研究包括制备方法、性能评估和DFT计算，展示了其在水处理技术中的功效（Liang et al., 2024）。
- 双感测探头发展：研制了一种新型的含2-肼吡啶的双氰异佛隆探针，用于近红外荧光双传感Zn(2+)和Cd(2+)。这一进步有助于检测和分析各种环境和生物样品中的重金属（Yan et al., 2023）。
- 赖氨酸氧化酶活性位点分析：该研究深入了解了赖氨酸氧化酶样2活性位点组分的空间排列，包括2-肼吡啶的作用，这对于理解酶的机制和潜在的治疗应用至关重要（Meier et al., 2022）。
- 赖氨酸氧化酶的结构分析：研究重点是预测赖氨酸氧化酶样2的胺氧化酶结构域的三维结构，探索2-肼吡啶促进的相互作用动力学。这对分子生物学和酶功能分析领域意义重大（Meier et al., 2022）。
警示用语：
Warning
危险声明
危险分类
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
靶器官
Respiratory system
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
230.0 °F - closed cup
闪点(°C)
110 °C - closed cup
个人防护装备
dust mask type N95 (US), Eyeshields, Gloves
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
J M Murray et al.
Biochemistry, 38(26), 8217-8227 (1999-07-01)
Amine oxidases utilize a proton abstraction mechanism following binding of the amine substrate to the C5 position of the cofactor, the quinone form of trihydroxyphenylalanine (TPQ). Previous work [Wilmot, C. M., et al. (1997) Biochemistry 36, 1608-1620] has shown that
Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential.
J M Murray et al.
Biochemistry, 40(43), 12808-12818 (2001-10-24)
Copper amine oxidases are homodimeric enzymes that catalyze two reactions: first, a self-processing reaction to generate the 2,4,5-trihydroxyphenylalanine (TPQ) cofactor from an active site tyrosine by a single turnover mechanism; second, the oxidative deamination of primary amine substrates with the
C M Wilmot et al.
Biochemistry, 36(7), 1608-1620 (1997-02-18)
The crystal structure of the complex between the copper amine oxidase from Escherichia coli (ECAO) and a covalently bound inhibitor, 2-hydrazinopyridine, has been determined to a resolution of 2.0 A. The inhibitor covalently binds at the 5 position of the
G De Matteis et al.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 4(3), 348-353 (1999-08-10)
Bovine serum amine oxidase (BSAO) reacts with 2-hydrazinopyridine, which binds the organic co-factor 2,4,5-trihydroxyphenylalanine quinone, forming a band at 435 nm. The band shifts to 526 nm around 60 degrees C, to 415 nm upon denaturation, but only shifts to
Minae Mure et al.
Biochemistry, 44(5), 1583-1594 (2005-02-03)
Adduct I (lambda(max) at approximately 430 nm) formed in the reaction of 2-hydrazinopyridine (2HP) and the TPQ cofactor of wild-type Escherichia coli copper amine oxidase (WT-ECAO) is stable at neutral pH, 25 degrees C, but slowly converts to another spectroscopically
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