B2753
氯化丁酰胆碱
≥98%
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关于此项目
线性分子式:
C9H20NO2Cl
化学文摘社编号:
分子量:
209.71
NACRES:
NA.22
PubChem Substance ID:
UNSPSC Code:
12352100
EC Number:
220-999-9
MDL number:
Assay:
≥98%
Form:
powder
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
Iu G Zhukovskiĭ et al.
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
Babiker Elamin
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
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
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
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
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