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Merck

C4290

Sigma-Aldrich

Butyrylcholinesterase from equine serum

lyophilized powder, ≥500 units/mg protein

Synonim(y):

Acylcholine acyl-hydrolase, Choline esterase, butyryl, Pseudocholinesterase

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About This Item

Numer CAS:
Numer EC enzymu:
Numer WE:
Numer MDL:
Kod UNSPSC:
12352204
NACRES:
NA.54

pochodzenie biologiczne

equine serum

Postać

lyophilized powder

aktywność właściwa

≥500 units/mg protein

skład

Protein, ≥10%

temp. przechowywania

−20°C

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Zastosowanie

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.

Działania biochem./fizjol.

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.

Definicja jednostki

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.

Postać fizyczna

Highly purified, lyophilized powder containing buffer salts

Komentarz do analizy

Protein determined by biuret
This page may contain text that has been machine translated.

inhibitor

Piktogramy

Health hazard

Hasło ostrzegawcze

Danger

Zwroty wskazujące rodzaj zagrożenia

Zwroty wskazujące środki ostrożności

Klasyfikacja zagrożeń

Resp. Sens. 1

Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 3

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

Eyeshields, Gloves, type N95 (US)


Certyfikaty analizy (CoA)

Poszukaj Certyfikaty analizy (CoA), wpisując numer partii/serii produktów. Numery serii i partii można znaleźć na etykiecie produktu po słowach „seria” lub „partia”.

Masz już ten produkt?

Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Determination of thyroxine binding globulin.
Bergmeyer, H.U
Methods of Enzymatic Analysis, 2, 833-833 (1974)
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
Physical properties and subunit structure of butyrylcholinesterase from horse serum.
J C Lee et al.
Biochemistry, 12(8), 1622-1630 (1973-04-10)
Acetylcholinesterase assay for cerebrospinal fluid using bupivacaine to inhibit butyrylcholinesterase
Kluge WH, et al.
BMC Biochemistry, 2(1), 17-17 (2001)
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

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