Comparison of methods used for the determination of cholinesterase activity in whole blood.

Abstract:

:Cholinesterases (ChEs) are classified as either acetylcholinesterase (AChE) or butyrylcholinesterase (BChE) based on their substrate and inhibitor specificity. Organophosphate and carbamate compounds commonly represented by herbicides, pesticides, and nerve gases irreversibly inhibit ChEs. Therefore, exposure to organophosphates and carbamates is normally assessed by measuring ChE activity in blood. There are two approaches for measuring AChE and BChE activity present in whole blood: (1) separating blood into erythrocytes, which contain only AChE, and plasma which contains only BChE, to measure their activity individually, or (2) use a BChE-specific inhibitor to measure the activity of AChE in whole blood. A number of studies have reported the use of different inhibitors for the simultaneous measurement of AChE and BChE activities. However, the inhibitors used for completely inhibiting BChE activity also inhibited AChE activity leading to errors in reported values. The goal of this study was to find the most accurate and simple method for the simultaneous determination of AChE and BChE activity in animal whole blood. Solutions containing human AChE and BChE in various proportions were prepared and AChE and BChE activities were measured using three reported methods. Results demonstrate that ethopropazine and (-) huperzine A appear to be the most specific ChE inhibitors. Preliminary results with human and animal whole blood suggest that 20 microM ethopropazine and 500 nM (-) huperzine A can be used for measuring AChE and BChE activities across species.

journal_name

Chem Biol Interact

authors

Naik RS,Doctor BP,Saxena A

doi

10.1016/j.cbi.2008.05.002

subject

Has Abstract

pub_date

2008-09-25 00:00:00

pages

298-302

issue

1-3

eissn

0009-2797

issn

1872-7786

pii

S0009-2797(08)00256-1

journal_volume

175

pub_type

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