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B22852

Sigma-Aldrich

Benzylhydrazine dihydrochloride

97%

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About This Item

Linear Formula:
C6H5CH2NHNH2 · 2HCl
CAS Number:
20570-96-1
Molecular Weight:
195.09
Beilstein:
3688990
EC Number:
243-887-1
MDL number:
MFCD00012921
UNSPSC Code:
12352100
PubChem Substance ID:
24891643
NACRES:
NA.22

Quality Level

200

Assay

97%

form

powder

mp

143-145 °C (dec.) (lit.)

SMILES string

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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Related Categories

Pictograms

Exclamation mark
GHS07

Signal Word

Warning

Hazard Statements

H315,H319,H335

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Sigma-Aldrich

152137

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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
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
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.
David B Langley et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 64(Pt 7), 577-583 (2008-07-09)
Complexes of Arthrobacter globiformis amine oxidase (AGAO) with the inhibitors benzylhydrazine and tranylcypromine (an antidepressant drug) have been refined at 1.86 and 1.65 A resolution, respectively. Both inhibitors form covalent adducts with the TPQ cofactor. A tyrosine residue, proposed to
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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