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Safety Information

C4290

Sigma-Aldrich

Butyrylcholinesterase from equine serum

lyophilized powder, ≥500 units/mg protein

Synonym(s):

Acylcholine acyl-hydrolase, Choline esterase, butyryl, Pseudocholinesterase

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About This Item

CAS Number:
9001-08-5
Enzyme Commission number:
3.1.1.8 (BRENDA, IUBMB)
EC Number:
232-579-2
MDL number:
MFCD00081455
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

equine serum

form

lyophilized powder

specific activity

≥500 units/mg protein

composition

Protein, ≥10%

storage temp.

−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.

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.

Unit Definition

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.

Physical form

Highly purified, lyophilized powder containing buffer salts

Analysis Note

Protein determined by biuret

inhibitor

Product No.
Description
Pricing

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

C4290-100UN:
C4290-5KU:
C4290-500UN:
C4290-BULK:
C4290-1KU:
C4290-VAR:

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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