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品質水準
アッセイ
≥98%
フォーム
powder
保管温度
−20°C
SMILES記法
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
保管分類コード
11 - Combustible Solids
WGK
WGK 3
引火点(°F)
Not applicable
引火点(℃)
Not applicable
適用法令
試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。
Jan Code
B2753-5G:
B2753-10G:
B2753-VAR:
B2753-BULK:
B2753-1G:
B2753-25G:
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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
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
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
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
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