A Method for Fast Assessment of OP/CB Exposure in the Japanese Quail (Coturnix coturnix japonica) Using Combined Esterases Enzyme Activity as Biomarkers
The aims of this study were to investigate the presence of different esterase activities in plasma and liver for Japanese quail and to combine determination of both carboxylesterase and cholinesterase as biochemical biomarker in order to identify the effects of carbamate and organophosphate compounds exposure. Carboxylesterase exhibits larger sensitivity to carbamate and organophosphate compounds than to cholinesterase and is present at higher levels. This permitted nature and distribution of carboxylesterase or cholinesterase to be measured. One predominant toxicological form of enzyme level constant in its patterns of motivation and inhibition with cholinesterase was identified in plasma with an apparent Michaelis constant for butyrylthiocholine iodide of 0.394？mM. Carboxylesterase activity in liver was considered by its preferential hydrolysis of the S-phenyl thioacetate. A concentration dependent decrease of carboxylesterase and cholinesterase has demonstrated during in vitro incubation of malathion, parathion, and trichlorfon in the range 0.125–2？mM, while with methomyl was in the range 0.25–4？mM. When quail ( ) was exposed orally for 48？h to concentrations of carbamate or organophosphate compounds of 3–200？mg/kg, the percentage inhibition of cholinesterase was in each case larger than that of carboxylesterase and reached statistical significance ( ) at lower concentrations. 1. Introduction Enzymes that preferentially catalyse the hydrolysis of ester bonds are classified as esterase (EC 3.1) and generally classified into two subgroups, carboxylesterase (CbE; EC 3.1.1.1) and cholinesterase (ChE; EC 3.1.1.7), depending on their substrate specificity and behaviour towards some inhibitors [1, 2]. There are many esterase decreases among carbamate (CB) and organophosphate (OP) compounds, which are the most important in the agriculture and veterinary medicine to control insect invasion; these compounds exert their toxic effects through inhibiting esterase enzyme activities [3–5]. CB and OP compounds exert acute toxicity by inhibition ChE, a serine hydrolase found in neuromuscular junctions of birds (connects the nervous system to the muscular system via synapses) as well as in peripheral and central cholinergic synapses [6, 7]. This leads to susceptible types in overaccumulation of the excitatory neurotransmitter acetylcholine and subsequent hyperpolarisation of the postsynaptic membrane. Determination of CbE and ChE enzyme activities levels is a valuable, dose dependent means of monitoring exposure to CB and OP pesticides in animal models and other
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