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Merck
CN

B22852

Sigma-Aldrich

苄基肼 二盐酸盐

97%

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线性分子式:
C6H5CH2NHNH2 · 2HCl
CAS号:
分子量:
195.09
Beilstein:
3688990
EC 号:
MDL编号:
UNSPSC代码:
12352100
PubChem化学物质编号:
NACRES:
NA.22

质量水平

检测方案

97%

形式

powder

mp

143-145 °C (dec.) (lit.)

SMILES字符串

Cl.Cl.NNCc1ccccc1

InChI

1S/C7H10N2.2ClH/c8-9-6-7-4-2-1-3-5-7;;/h1-5,9H,6,8H2;2*1H

InChI key

MSJHOJKVMMEMNX-UHFFFAOYSA-N

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象形图

Exclamation mark

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

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

dust mask type N95 (US), Eyeshields, Gloves


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D J Merkler et al.
Archives of biochemistry and biophysics, 317(1), 93-102 (1995-02-20)
Peptidylglycine alpha-amidating enzyme catalyzes the two-step conversion of C-terminal glycine-extended peptides to C-terminal alpha-amidated peptides and glyoxylate in a reaction that requires O2, ascorbate and 2 mol of copper per mole of enzyme [Kulathila et al. (1994) Arch. Biochem. Biophys.
A Bellelli et al.
European journal of biochemistry, 267(11), 3264-3269 (2000-05-29)
The presteady-state and steady-state kinetics of bovine serum amine oxidase (BSAO) were analyzed by stopped-flow transient spectroscopy. A simplified model of the catalytic cycle was found to describe the experimental data and the rate constants of the individual steps were
L Morpurgo et al.
The Biochemical journal, 260(1), 19-25 (1989-05-15)
Bovine serum amine oxidase is inhibited by benzylhydrazine (BHy), but recovers full activity after a few hours incubation [Hucko-Haas & Reed (1970) Biochem. Biophys. Res. Commun. 38, 396-400]. The first phase of the process, requiring about 15 min, was found
L Morpurgo et al.
Biology of metals, 3(2), 114-117 (1990-01-01)
The role of copper in bovine serum amine oxidase was investigated by studying the effect of copper-binding inhibitors on the reactions of the pyrroloquinoline quinone carbonyl and on the reaction with oxygen. Hydrazines and hydrazides were used as carbonyl reagents
F N Bolkenius et al.
Biochemical pharmacology, 53(11), 1695-1702 (1997-06-01)
Peptidylglycine alpha-hydroxylating monooxygenase (PHM; EC 1.14.17.3) catalyses the rate-limiting step in the post-translational activation of substance P, among other neuropeptides, from its glycine-extended precursor. Comparative kinetic studies were performed, using trans-styrylacetic acid or trans-styrylthioacetic acid as known mechanism-based inhibitors, of

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