Recommended Products
Assay
≥98%
form
powder
storage temp.
−20°C
SMILES string
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
InChI key
VCOBYGVZILHVOO-UHFFFAOYSA-M
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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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
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
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
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
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
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