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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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
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
Ukrainskii biokhimicheskii zhurnal (1978), 67(4), 40-46 (1995-07-01)
Cetyltrimethyl ammonium and cetylpyridinium, both being cationic detergents, have been studied for their effect on the catalytic activity of horse blood serum cholinesterase (BuHChE) in reactions of hydrolysis of carbonic acid esters. It is shown that the detergents tested are
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
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
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