InChI key
VCOBYGVZILHVOO-UHFFFAOYSA-M
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
SMILES string
O.[Cl-].CCCC(=O)OCC[N+](C)(C)C
assay
≥98%
form
powder
storage temp.
−20°C
Quality Level
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
M Watanabe et al.
Biochemical medicine and metabolic biology, 36(3), 355-362 (1986-12-01)
Acetylcholine levels of whole blood from 80 healthy subjects were determined by pyrolysis-gas chromatography-mass fragmentography. Acetylcholine was extracted from 1.2 ml of venous blood in the presence of eserine, demethylated by pyrolysis, and assayed by selected ion-current monitoring using butyrylcholine
M Chelminska-Bertilsson et al.
Biochimica et biophysica acta, 1202(1), 56-60 (1993-09-03)
The hydrolysis of long-chain alkanoylcholines catalyzed by butyrylcholinesterase (EC 3.1.1.8) has been studied. Radiolabelled substrates have been used and a radiochromatographic detection method developed earlier has been applied. The long-chain choline esters were found to be excellent substrates for butyrylcholinesterase
J Stojan
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
Elmorsy Khaled et al.
Talanta, 83(2), 357-363 (2010-11-30)
A highly sensitive disposable screen-printed butyrylcholine (BuCh) potentiometric sensor, based on heptakis (2,3,6-tri-o-methyl)-β-cyclodextrin (β-CD) as ionophore, was developed for butyrylcholinesterase (BuChE) activity monitoring. The proposed sensors have been characterized and optimized according to the constituents of homemade printing carbon ink
A L Gindilis et al.
Prikladnaia biokhimiia i mikrobiologiia, 34(3), 326-331 (1998-06-30)
Potentiometric choline electrodes were developed on the basis of the mediator-free bioelectrocatalysis. The electrodes made of a composite carbon-polymer material contain choline oxidase and peroxidase coimmobilized on the surface of the electrode. The rate of the potential increase was shown
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