Hydrolysis of acetylcholinesterase inhibitors--organophosphorus acid anhydrolase enzyme immobilization on photoluminescent porous silicon platforms.
نویسندگان
چکیده
We report on the immobilization of an OPAA enzyme on luminescent porous silicon devices, and on the utilization of this new platform to hydrolyze p-nitrophenyl-soman.
منابع مشابه
Enzyme-based biosensor for the direct detection of fluorine-containing organophosphates
The ability of the enzyme organophosphorus acid anhydrolase (OPAA) to selectively hydrolyze the P–F bond of fluorine containing organophosphates has been used to develop a biosensor for specific detection of these compounds. Hydrolysis rate of diisopropyl fluorophosphate (DFP), paraoxon and demeton-S, by soluble and immobilized OPAA was measured. These compounds were selected as representative ...
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Acetylcholinesterase is involved in the termination of impulse transmission by rapid hydrolysis of the neurotransmitter acetylcholine in numerous cholinergic pathways in the central and peripheral nervous systems. The enzyme inactivation, induced by various inhibitors, leads to acetylcholine accumulation, hyperstimulation of nicotinic and muscarinic receptors, and disrupted neurotransmission. H...
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A successful prescription is presented for acetylcholinesterase physically adsorbed on to a mesoporous silicon surface, with a promising hydrolytic response towards acetylthiocholine iodide. The catalytic behaviour of the immobilized enzyme was assessed by spectrophotometric bioassay using neostigmine methyl sulfate as a standard acetycholinesterase inhibitor. The surface modification was studi...
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Nerve agent-degrading enzymes Organophosphorus Acid Anhydrolase (OPAA) and Organophosphorus Hydrolase (OPH) covalently-coupled to solid supports were examined as drinking water system nerve agent decontaminants. Enzymes were bound to azlactone polyacrylamide, glyoxal agarose and glyoxal-aminopropyl controlled-pore glass and tested for stability in unbuffered tap water. Kinetic analyses showed t...
متن کاملSubstrate and stereochemical specificity of the organophosphorus acid anhydrolase from Alteromonas sp. JD6.5 toward p-nitrophenyl phosphotriesters.
The enzyme OPAA hydrolyzes p-nitrophenyl phosphotriesters bearing substituents at the phosphorus center ranging in size from methyl to phenyl. The enzyme exhibits stereoselectivity toward the hydrolysis of chiral substrates with a preference for the Sp enantiomer.
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ورودعنوان ژورنال:
- Chemical communications
دوره 7 شماره
صفحات -
تاریخ انتشار 2005