In-vitro Modification of Acetylcholinesterase activity in adult head of Zonocerus variegatus: a biomarker to effects of most chemical agents.

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ABSTRACT

Acetylcholinesterase(AChE) is the key cholinesterase in the body which catalyzes the breakdown of acetylcholine and some other choline esters that functions as neurotransmitter in living cell. It belongs to the carboxyl esterase (hydrolase) family of enzymes which are found mainly at the neuromuscular junction (point of contact between the nervous system and the muscles) and the chemical synapses of the cholinergic types. It functions to terminate synaptic transmission by breaking down the neurotransmitter, acetylcholine, into acetate and choline. The head of the Zonocerus variegatus adult was used during the course of this study as the source of enzyme. Crude enzyme obtained was purified using ion – exchange chromatography, and protein concentration and enzyme activities was determined. Acetylcholinesterase modification is a significant biomarker of the effects of most chemical agents. The extent of modification of AChE with varying concentration of N-BromoSuccinamide(NBS) was used in this study. By extrapolation of the modified residue- enzymatic activity to a less inactive state, it was found that modification of some tryptophan residues is responsible for the reduction in enzymes activity. It seems therefore that tryptophan residues are involved in the active site or near the active site of the acetylcholinesterase from the adult head of the Zonocerus variegatus.

Keywords: Acetylcholinesterase, N-BromoSuccinamide, Acetylcholinesterase modification, Acetylcholine, Enzymatic activity, Zonocerus variegatus.

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