• Toxicological Research
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• v.6 no.1
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• pp.51-59
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• 1990

Effects of altering hepatic mixed-function oxidase (MFO) enzyme activities on the metabolism and acute toxicity of parathio were investigated in adult female rats. In vitro hepatic metabolism of parathion to paraoxon was increased by phenobarbital pretreatment (50 mg/kg/day, ip, for 4 consecutive days) and SKF 525-A (50 mg/kg, ip, 1 hr prior to sacrifice) decreased paraoxon formation indicating that phenobarbital induces that form(s) of cytochrome P-450 catalyzing conversion of parathion to paraoxon. Degradation of paraoxon to p-nitrophenol was increased by phenobarbital pretreatment, but not affected by SKF 525-A suggesting that MFO activities play only a minor role in the detoxification of the active metabolite of this insecticide. The phenobarbital-induced increase in paraoxon formation was partially antagonized by SKF 525-A. Significant activity for both parathion activation and paraoxon degradation was also observed in the lung preparation, however, this extrahepatic parathion and paraoxon metabolizing activity was not induced by phenobarbital or inhibited by SKF 525-A pretreatment. Phenobarbital pretreatment increased paraoxon level in livers of rats when measured 3 hr following parathion injection (2 mg/kg, ip). SKF 525-A did not alter parathion or paraoxon levels in brain, blood and liver. Phenobarbital pretreatment decreased the toxicity of parathion (4mg/kg, ip) or paraoxon (1.5 mg/kg, ip) as determined by decreases in lethality and inhibition of brain and lung acetylcholinesterases. An additional SKF 525-A treatment failed to decrease the protective effects of phenobarbital against parathion or paraoxon toxicity. These results suggest that some unknown factors other than hepatic MFO induction are involved in the protective action of phenobarbital against parathion and paraoxon toxicity.

• Journal of the Korea Organic Resources Recycling Association
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• v.14 no.3
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• pp.110-116
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• 2006

In this study, the biodegradation rate of paraoxon, that is an organophosphate pesticide, was enhanced by recombinant Escherichia coli harboring organophosphorus hydrolase (OPH). The optimum conditions were 8.5 of initial pH and 5.0% of acetone for the enhancement of specific whole cell OPH activity. When the OPH was produced to 498 Unit/L, 98% of 275mg/L paraoxon was degraded within 10 minutes, and thus the biodegradation rate was enhanced to $29.2mg/g{\cdot}min$. The results implied that practical bioremediation technology developed in this study was an effective method to degrade residual organophosphate pesticide in ground water or soils in a short time.

• Bulletin of the Korean Chemical Society
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• v.34 no.12
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• pp.3855-3858
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• 2013

• Journal of Sensor Science and Technology
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• v.22 no.5
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• pp.346-351
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• 2013

We developed a one-step method for fabrication of addressable suspended SWNT films and demonstrate excellent detection performance of paraoxon based on OPH-immobilized SWNT films for environmental monitoring. For dispersed SWNT suspension, COOH-SWNT was prepared by the oxidation of carbon nanotubes using acid treatment and sonication. Suspended SWNT-film was fabricated between cantilever electrodes by dielectrophoretic force and surface tension of the water meniscus. After that, OPH were immobilized on suspended SWNT-films by nonspecific binding for enzymatic hydrolysis of paraoxon. The electrical properties of the SWNT films were measured in real time at room temperature. Structurally suspended SWNT films from substrate surface made possible rapid and highly sensitive detection of target molecules with increased convectional and diffusional fluxes of the molecules and with a large binding surface area. SWNT film FET resulted in a real-time, label-free, and electrical detection of paraoxon to the concentration of ca. $10{\mu}m$ with a step-wise rapid response time of several seconds.

• Bulletin of the Korean Chemical Society
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• v.27 no.9
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• pp.1401-1404
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• 2006

Eight structurally different acetylcholinesterase reactivators derived from currently commercially available oximes were tested for their potency to reactivate acetylcholinesterase inhibited by pesticide paraoxon (P) and DFP (D). Housefly AChE (F) and bovine red blood cell AChE (B) were used as the source of the cholinesterases. Ellman's method was taken to examine cholinesterases activity. The results show that four AChE reactivators are potent AChE reactivators, able to reach reactivation potency of more than 30% in all cases - PF, PB, DF and DB. Their reactivation potency was comparable with that of pralidoxime and even higher compared with that of HI-6, standard AChE reactivators currently available on the market.

• Toxicological Research
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• v.17 no.4
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• pp.303-308
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• 2001

The potential for a given anticholinesterase pesticide to exhibit age-related toxicity is essential information for an accurate and proper risk assessment of that compound. This investigation was designed to study the age-related toxicity of active metabolites of four organophosphates using in vitro detoxification measurement. The blood samples were collected from 1 month and 18 months old rats. The $IC_{50}$ values of mouse brain recombinant AChE of chlorpyrifos-oxon, diazoxon, malaoxon and paraoxon were 10.35, 112.84, 151.28 and 18.43 nM, respectively. When the plasma of young rats, and $CaCI_2$were added, the $IC_{50}$ values of mouse brain recombinant AChE of chlorpyrfos-oxon, diazoxon, malaoxon and paraoxon were 31.89, 164.25, 139.94 and 16.36 nM, respectively. The $IC_{50}$ values of mouse brain recombinant AChE of chlorpyrifos-oxon, diazoxon, malaoxon and paraoxon were changed to 136.840, 1244.45, 654.54 and 52.66 nM by A-esterases In adult rats. These results suggest that four organophosphates have a potential toxicity to exhibit age-related sensitivity.

• Proceedings of the PSK Conference
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• 2003.10b
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• pp.141.1-141.1
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• 2003

Paraoxonase, an antioxidant enzyme, exclusively located on HDL is well known for both hydrolysis of organophosphate and prevention against LDL oxidation. It have been reported that PON1 decrease its activity under oxidative stress and that PON1 activity is lower in subject with higher vulnerability to organophosphate poisoning. The aim of our study is to examine the effect of oxidative system on paraoxon-hydrolzing activity and to elucidate the plausible mechanisms responsible for the decline of HDL-asscociated PON1 activity in vivo system. (omitted)

• Journal of the Korea Organic Resources Recycling Association
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• v.13 no.3
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• pp.89-96
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• 2005

In the present work, production of organophosphorus hydrolase (OPH) that is secreted in periplasmic space of recombinant Escherichia coli was performed for degradation of environmental toxic organophosphate compounds, paraoxon. The optimal conditions for enhancement of OPH production were 1.0 mM isopropyl-${\beta}$-D-thiogalactopytanoside (IPTG), 0.25 mM $Co^{2+}$, and 0.1 mM ethylenediamine tetraacetate (EDTA). Under these culture conditions, the maximum OPH production was $174Unit/L{\cdot}OD$. In addition, 1 mM of paraoxon was completely degraded by OPH. These results can be used as a bioremediation tool for removal of environmental toxic organophosphate compounds remaining in soil and aquatic environment.

• KSBB Journal
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• v.17 no.2
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• pp.158-161
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• 2002

In this study, a prototype fiber-optic biosensor was fabricated using the inhibition of enzyme reaction by organophosphorus compounds to detect organophosphorus compounds, which is nervous toxic material an? is used as chemical weapon and pesticide. Enzyme, substrate, and inhibitor for enzyme reaction were acetylcholinesterase (key enzyme in nervous cell), acetylthiocholine iodide, and paraoxon (a kind of organophosphorus compounds), respectively. The detection principle of sensor is the detection of enzyme reaction inhibited by organophosphorus compounds by the quantitative measurement of acetic acid, which was achieved by absorbance measurement using litmus solution that maximum absorbance band is changed by pH. To fabricate prototype fiber-optic biosensor, high bright LED and photodiode was used as light source and light intensity detector, respectively. From the experimental results using a prototype biosensor, the linear change of sensor signal was obtained in a range of 0-2 ppm inhibitor concentrations. From these results, it was verified that the quantitative measurement of organophosphorus compounds could be achieved fast (within 2 minutes) and accurately by a prototype fiber-optic biosensor.

• Bulletin of the Korean Chemical Society
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• v.31 no.6
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• pp.1609-1614
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• 2010

Acetylcholinesterase reactivators are crucial antidotes for the treatment of organophosphate intoxication. Standard in vitro test was chosen using a rat brain homogenate as the source of AChE. Screening of reactivation potency was performed with two concentration of reactivator (1000 ${\mu}M$ and 10 ${\mu}M$). Results were compared to established reactivators pralidoxime, methoxime, HI-6, trimedoxime and obidoxime. More than 30 novel reactivators performed equal or better reactivation ability of POX-inhibited AChE compared to currently used reactivators. The structure-activity relationship for reactivators of paraoxon-inhibited AChE was developed.