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EN
Chiral effects for the inhibition of acetylcholinesterase by organophosphorus pesticides were investigated for insecticide malathion and malaoxon, which is a metabolic product of malathion in living organisms. Studies were carried out using a bienzymatic biosensor with immobilized acetylcholinesterase, choline oxidase, and with Prussian Blue used as a mediator. In both cases the R enantiomers accelerate acetylocholinesterase inhibition. The chiral effect in inhibition was much more pronounced in fast flow measurements than in batch measurements. [...]
2
Content available remote Inactivation of cholinesterases by silver and gold ions in vitro
100%
Open Chemistry
|
2013
|
tom 11
|
nr 6
935-944
EN
The main goal of the present study was to investigate the effects of silver and gold ions on cholinesterases (ChEs) activity due to increasing application of these metals in a wide variety of nanomaterials. A chromogenic assay using the substrate o-nitrophenyl acetate/butyrate made it possible to conclude unmistakably that both metals inhibit ChEs. Addition of bovine serum albumin (BSA) indicates that binding of metal ions to albumin could serve to scavenge metals and consequently reduce their amount for reaction with ChEs. The effects of metal ions on ChE should be taken into consideration when using this enzyme as an environmental biomarker. [...]
3
100%
EN
The immobilisation of AChE enzyme through chemisorption on Au-modified graphite was examined with view of its prospective application in the design of membraneless electrochemical biosensors for the assay of enzyme inhibitors. The developed immobilisation protocol has been based on a two-stage procedure, comprising i) electrodeposition of gold nanostructures on spectroscopic graphite; followed by ii) chemisorption of the enzyme onto gold nanoparticles. Both the coverage of the electrode surface with Au nanostructures and the conditions for enzyme immobilisation were optimised. The proposed electrode architecture together with the specific type of enzyme immobilisation allow for a long-term retaining of the enzyme catalytic activity. The extent of inhibition of the immobilised acetylcholinesterase enzyme by the organophosphorous compound monocrotophos has been found to depend linearly on its concentration over the range from 50 to 400 nmol mL−1 with sensitivity 77.2% inhibition per 1 µmol mL−1 of monocrotophos. [...]
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