C4290
Butyrylcholinesterase from equine serum
lyophilized powder, ≥500 units/mg protein
Synonyme(s) :
Acylcholine acyl-hydrolase, Choline esterase, butyryl, Pseudocholinesterase
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About This Item
Produits recommandés
Source biologique
equine serum
Forme
lyophilized powder
Activité spécifique
≥500 units/mg protein
Composition
Protein, ≥10%
Température de stockage
−20°C
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Application
Butyrylcholinesterase (BChE) from equine serum has been used:
- to determine the inhibitory concentration of bupivacaine on butyrylcholinesterase
- in acetylcholinesterase (AChE)/BChE activity assay to determine the inhibitory activity of benzothiazole-piperazine compounds
Selective inhibition of BChE activity can be used in the detection of organophosphates. Its use in the treatment of organophosphate toxicity shows promise. There is a correlation between the level of BChE in human blood and degree of protection against potentially toxic nerve agents. There has also been interest in the roles of cholinesterases with regard to Alzheimer′s disease. Investigations into selective inhibitors may provide a clearer picture of the physiological role of BChE in both healthy and diseased individuals. The enzyme has been used to test bupivacaine as an inhibitor of butyrylcholinesterase during acetylcholinesterase assay using cerebrospinal fluid.
Actions biochimiques/physiologiques
Butyrylcholinesterase (BChE) is a serine hydrolase that is structurally similar to acetylcholinesterase (AChE), but differs in substrate specificities and inhibitor sensitivities. BChE can, unlike AChE, efficiently hydrolyze larger esters of choline such as butyrylcholine and benzoylcholine. The enzyme is a tetrameric glycoprotein with four equal subunits (110 kDa each). The enzyme is activated by Ca2+ and Mg2+ and the activity is constant over the pH range 6.0-8.0. It is inhibited by Betaine, nicotine, organophosphates, carbamates.
Définition de l'unité
One unit will hydrolyze 1.0 μmole of butyrylcholine to choline and butyrate per min at pH 8.0 at 37 °C. The activity obtained using butyrylcholine as substrate is ~2.5 times that obtained using acetylcholine.
Forme physique
Highly purified, lyophilized powder containing buffer salts
Remarque sur l'analyse
Protein determined by biuret
Inhibiteur
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Resp. Sens. 1
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
Certificats d'analyse (COA)
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Les clients ont également consulté
W H Kluge et al.
BMC biochemistry, 2, 17-17 (2002-01-22)
Most test systems for acetylcholinesterase activity (E.C.3.1.1.7.) are using toxic inhibitors (BW284c51 and iso-OMPA) to distinguish the enzyme from butyrylcholinesterase (E.C.3.1.1.8.) which occurs simultaneously in the cerebrospinal fluid. Applying Ellman's colorimetric method, we were looking for a non-toxic inhibitor to
Luisa Savini et al.
Journal of medicinal chemistry, 46(1), 1-4 (2002-12-28)
Tacrine-based AChE and BuChE inhibitors were designed by investigating the topology of the active site gorge of the two enzymes. The homobivalent ligands characterized by a nitrogen-bridged atom at the tether level could be considered among the most potent and
Acetylcholinesterase assay for cerebrospinal fluid using bupivacaine to inhibit butyrylcholinesterase
Kluge WH, et al.
BMC Biochemistry, 2(1), 17-17 (2001)
Physical properties and subunit structure of butyrylcholinesterase from horse serum.
J C Lee et al.
Biochemistry, 12(8), 1622-1630 (1973-04-10)
Stefano Cinti et al.
Nature protocols, 14(8), 2437-2451 (2019-07-05)
Despite substantial advances in sensing technologies, the development, preparation, and use of self-testing devices is still confined to specialist laboratories and users. Decentralized analytical devices will enormously impact daily lives, enabling people to analyze diverse clinical, environmental, and food samples
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