B2753
Butyrylcholine chloride
≥98%
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About This Item
Productos recomendados
Análisis
≥98%
formulario
powder
temp. de almacenamiento
−20°C
cadena SMILES
O.[Cl-].CCCC(=O)OCC[N+](C)(C)C
InChI
1S/C9H20NO2.ClH/c1-5-6-9(11)12-8-7-10(2,3)4;/h5-8H2,1-4H3;1H/q+1;/p-1
Clave InChI
VCOBYGVZILHVOO-UHFFFAOYSA-M
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Certificados de análisis (COA)
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Amide derivatives of N-phthaloylglycine were synthesized under Schotten Baumann reaction condition. The structures of synthesized compounds (4a-d) were characterized by using FTIR, 1HNMR and EI-MS. The compounds were evaluated for their in-vitro Butyrylcholinesterase inhibition and all of them exhibited good
Journal of enzyme inhibition, 14(3), 193-201 (1999-08-13)
Acetylcholinesterases from Drosophila melanogaster and Torpedo marmorata possess 35% identical residues. We built a homology model of the Drosophila enzyme on the basis of the known three-dimensional structure of Torpedo acetylcholinesterase, which revealed an oval rim of the active site
Clinica chimica acta; international journal of clinical chemistry, 203(2-3), 295-303 (1991-12-16)
A simple method for the separate determination of acetylcholinesterase and butyrylcholinesterase activities in amniotic fluid is reported. This determination is performed with an enzyme electrode involving an immobilized choline oxidase membrane associated with the amperometric detection of hydrogen peroxide. Acetylcholine
Chemical communications (Cambridge, England), (8)(8), 971-973 (2009-02-14)
A novel reagentless biosensor has been developed in which the traditional ion selective electrode is used as a controlled-release system for in situ generation and detection of enzyme substrates.
Journal of biochemistry and molecular biology, 36(2), 149-153 (2003-04-12)
The dibucaine number (DN) was determined for serum cholinesterase (EC 3.1.1.8, SChE) in plasma samples. The ones with a DN of 79-82 were used, because they had the "usual" SChE variant. The enzyme was assayed colorimetrically by the reaction of
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