نتایج جستجو برای: paraoxon

تعداد نتایج: 783  

2008
Xueheng Zhao Xiaoke Hu Huey-Min Hwang

Abstract: Organophosphorus pesticides (OPs) and their transformation products become a concern when these compounds are released into the environment. To understand the effects of these pesticides on human health, toxicity of a widely used organophosphorus pesticide, parathion and its transformation products, i.e. paraoxon and 4-nitrophenol, were investigated by using T4 lymphocyte cells and Ha...

Journal: :The Biochemical journal 2013
Zoran Radić Trevor Dale Zrinka Kovarik Suzana Berend Edzna Garcia Limin Zhang Gabriel Amitai Carol Green Božica Radić Brendan M Duggan Dariush Ajami Julius Rebek Palmer Taylor

In the present paper we show a comprehensive in vitro, ex vivo and in vivo study on hydrolytic detoxification of nerve agent and pesticide OPs (organophosphates) catalysed by purified hBChE (human butyrylcholinesterase) in combination with novel non-pyridinium oxime reactivators. We identified TAB2OH (2-trimethylammonio-6-hydroxybenzaldehyde oxime) as an efficient reactivator of OP-hBChE conjug...

Journal: :Applied biochemistry and biotechnology 1991
S R Caldwell F M Raushel

A partially purified phophotriesterase was successfully immobilized onto nylon 6 and 66 membranes, nylon 11 powder, and nylon tubing. Up to 9000 U of enzyme activity was immobilized onto 2000 cm2 of a nylon 6 membrane where 1 U is the amount of enzyme necessary to catalyze the hydrolysis of 1.0 mumol of paraoxon/min at 25 degrees C. The nylon 66 membrane-bound phosphotriesterase was characteriz...

Journal: :Biosensors & bioelectronics 2001
P Mulchandani W Chen A Mulchandani J Wang L Chen

An amperometric microbial biosensor for the direct measurement of organophosphate nerve agents is described. The sensor is based on a carbon paste electrode containing genetically engineered cells expressing organophosphorus hydrolase (OPH) on the cell surface. OPH catalyzes the hydrolysis of organophosphorus pesticides with p-nitrophenyl substituent such as paraoxon, parathion and methyl parat...

2006
Joseph J. DeFrank

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...

Journal: :Insect biochemistry and molecular biology 2002
A Tsagkarakou N Pasteur A Cuany C Chevillon M Navajas

We investigated the mechanisms conferring resistance to methyl-parathion (44-fold) and to methomyl (8-fold) in Tetranychus urticae from Greece by studying the effect of synergists on the resistance and the kinetic characteristics of various enzymes in a resistant strain (RLAB) and a susceptible reference strain (SAMB). It is shown that S,S,S-tributyl phosphorotrithioate, a synergist that inhibi...

Journal: :Biochemistry 1999
S B Hong F M Raushel

A series of achiral, chiral, and racemic mixtures of paraoxon analogues containing various combinations of methyl, ethyl, isopropyl, or phenyl substituents were synthesized as probes of the stereochemical constraints within the active site of phosphotriesterase. The kinetic constants for these paraoxon analogues with the enzyme varied significantly with the size of substituents surrounding the ...

Journal: :Cancer research 1981
J B Vaught P B McGarvey M S Lee C D Garner C Y Wang E M Linsmaier-Bednar C M King

N-Hydroxyphenacetin was activated to a mutagen in the Salmonella-Ames test by rabbit liver acyltransferase, rat liver cytosol, and rat liver microsomes. N-[ring]3H]-Hydroxyphenacetin was bound to transfer RNA when activated by acyltransferase from rabbit or rat liver or rat liver microsomes. The acyltransferase-catalyzed binding was not inhibited by paraoxon, a deacetylase inhibitor. The use of...

Journal: :The Journal of biological chemistry 1989
D P Dumas S R Caldwell J R Wild F M Raushel

The phosphotriesterase produced from the opd cistron of Pseudomonas diminuta was purified 1500-fold to homogeneity using a combination of gel filtration, ion exchange, hydrophobic, and dye matrix chromatographic steps. This is the first organophosphate triesterase or organophosphofluoridate hydrolyzing enzyme to be purified to homogeneity. The enzyme is a monomeric, spherical protein having a m...

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