نتایج جستجو برای: paraoxon

تعداد نتایج: 783  

Journal: :Chemico-biological interactions 2013
Stephen D Kirby Joseph R Norris J Richard Smith Brian J Bahnson Douglas M Cerasoli

Variants of human paraoxonase 1 (PON1) are being developed as catalytic bioscavengers for the organophosphorus chemical warfare agents (OP). It is preferable that the new PON1 variants have broad spectrum hydrolase activities to hydrolyze both G- and V-class OPs. H115W PON1 has shown improvements over wild type PON1 in its capacity to hydrolyze some OP compounds. We improved upon these activiti...

Journal: :Journal of the American Chemical Society 2011
Isaac N Ugwumba Kiyoshi Ozawa Zhi-Qiang Xu Fernanda Ely Jee-Loon Foo Anthony J Herlt Chris Coppin Sue Brown Matthew C Taylor David L Ollis Lewis N Mander Gerhard Schenk Nicholas E Dixon Gottfried Otting John G Oakeshott Colin J Jackson

The bacterial phosphotriesterases catalyze hydrolysis of the pesticide paraoxon with very fast turnover rates and are thought to be near to their evolutionary limit for this activity. To test whether the naturally evolved turnover rate could be improved through the incorporation of unnatural amino acids and to probe the role of peripheral active site residues in nonchemical steps of the catalyt...

Journal: :Toxicology in vitro : an international journal published in association with BIBRA 2011
Marion Ehrich Roger Van Tassell Yunbo Li Zhiguo Zhou Chris L Kepley

Although organophosphate (OP)-induced acetylcholinesterase (AChE) inhibition is the critical mechanism causing toxicities that follow exposure, other biochemical events, including oxidative stress, have been reported to contribute to OP toxicity. Fullerenes are carbon spheres with antioxidant activity. Thus, we hypothesized that fullerenes could counteract the effects of OP compounds and tested...

Journal: :Environmental science & technology 2001
P Mulchandani W Chen A Mulchandani

A flow injection amperometric biosensor for the determination of organophosphate nerve agents was developed. The biosensor incorporated an immobilized enzyme reactor that contains the enzyme organophosphorus hydrolase covalently immobilized on activated aminopropyl controlled pore glass beads and an electrochemical flow-through detector containing carbon paste working electrode, a silver/silver...

Journal: :Journal of enzyme inhibition and medicinal chemistry 2002
Graziella L Turdean Ionel Catalin Popescu Liviu Oniciu Daniel R Thevenot

An acetylcholinesterase (AChE) based amperometric bioelectrode for a selective detection of low concentrations of organophosphorus pesticides has been developed. The amperometric needle type bioelectrode consists of a bare cavity in a PTFE isolated Pt-Ir wire, where the AChE was entrapped into a photopolymerised polymer of polyvinyl alcohol bearing styrylpyridinium groups (PVA-SbQ). Cyclic volt...

Journal: :RSC advances 2014
Xiude Hua Xiaofeng Liu Haiyan Shi Yanru Wang Hee Joo Kim Shirley J Gee Minghua Wang Fengquan Liu Bruce D Hammock

An enzyme-linked immunosorbent assay (ELISA) was developed to detect organophosphorus pesticides using a phage-borne peptide that was isolated from a cyclic 8-residue peptide phage library. The IC50 values of the phage ELISA ranged from 1.4 to 92.1 μg L-1 for eight organophosphorus pesticides (parathion-methyl, parathion, fenitrothion, cyanophos, EPN, paraoxon-methyl, paraoxon, fenitrooxon). Th...

Journal: :The Analyst 2016
Souksanh Nouanthavong Duangjai Nacapricha Charles S Henry Yupaporn Sameenoi

We report the first use of a paper-based device coated with nanoceria as a simple, low-cost and rapid detection platform for the analysis of organophosphate (OP) pesticides using an enzyme inhibition assay with acetylcholinesterase (AChE) and choline oxidase (ChOX). In the presence of acetylcholine, AChE and ChOX catalyze the formation of H2O2, which is detected colorimetrically by a nanoceria-...

Journal: :Biochimica et biophysica acta 2004
David T Yeung Denis Josse James D Nicholson Akhil Khanal Christopher W McAndrew Brian J Bahnson David E Lenz Douglas M Cerasoli

Human serum paraoxonase (HuPON1) is a calcium-dependent enzyme that hydrolyzes esters, including organophosphates and lactones, and exhibits anti-atherogenic properties. A few amino acids have been shown to be essential for the enzyme's arylesterase and organophosphatase activities. Until very recently, a three-dimensional model was not available for HuPON1, so functional roles have not been as...

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