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C4290

Butyrylcholinesterase from equine serum

lyophilized powder, ≥500 units/mg protein

Synonyme(s) :

Acylcholine acyl-hydrolase, Choline esterase, butyryl, Pseudocholinesterase

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A propos de cet article

Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-579-2
MDL number:
Numéro CE :
Specific activity:
≥500 units/mg protein
Biological source:
equine serum
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biological source

equine serum

Quality Level

form

lyophilized powder

specific activity

≥500 units/mg protein

composition

Protein, ≥10%

storage temp.

−20°C

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[1]

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.[2] 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.[3] The enzyme has been used to test bupivacaine as an inhibitor of butyrylcholinesterase during acetylcholinesterase assay using cerebrospinal fluid.[4]

Biochem/physiol Actions

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.

Physical form

Highly purified, lyophilized powder containing buffer salts

Analysis Note

Protein determined by biuret

Other Notes

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.

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Cet article
C1057SRE0020C7512
biological source

equine serum

biological source

-

biological source

-

biological source

-

specific activity

≥500 units/mg protein

specific activity

≥900 units/mg protein

specific activity

≥900 units/mg protein

specific activity

≥10 units/mg protein

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

200

Quality Level

300

Quality Level

400

Quality Level

200

composition

Protein, ≥10%

composition

Protein, ≥10%

composition

-

composition

Protein, ≥60%


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pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Classe de stockage

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)



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Contenu apparenté


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
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



Numéro d'article de commerce international

RéférenceGTIN
C4290-1KU04061833491966

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