• Toxicological Research
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• 제6권1호
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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.

• 유기물자원화
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• 제14권3호
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• pp.110-116
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• 2006

본 연구에서는 재조합 대장균으로 부터 Organophosphorus Hydrolase (OPH)를 이용하여 유기인 살충제 화합물인 paraoxon의 생분해 속도를 향상시켰다. OPH의 비 활성도 (Specific whole cell OPH Activity)를 증가시키기 위한 배지의 최적 조건은 초기 pH 8.5의 조절과 5.0 % acetone 첨가가 필요하다는 것을 알 수 있었다. 또한, 이 최적의 조건에서 498 Unit/L의 OPH가 생산될 때, 275 mg/L paraoxon은 반응 10분 동안 98% 생분해 효율을 나타내었고, 그 결과 생분해 속도를 $29.2mg/g{\cdot}min$까지 향상시킬 수 있었다. 이러한 실험 결과들은 지하수 또는 토양에 잔류하는 유기인 살충제를 빠른 시간 안에 효과적으로 생분해시키는 실질적인 생물 복원 기술로 사용될 수 있을 것이다.

• Bulletin of the Korean Chemical Society
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• 제34권12호
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• pp.3855-3858
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• 2013

• 센서학회지
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• 제22권5호
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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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• 제27권9호
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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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• 제17권4호
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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.

• 대한약학회:학술대회논문집
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• 대한약학회 2003년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2-2
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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)

• 유기물자원화
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• 제13권3호
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• pp.89-96
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• 2005

본 연구에서는 유기인 화합물인 Paraoxon의 분해를 위하여 재조합 대장균에서 세포내 간극(periplasmic space)으로 분비되는 organophosphorus hydrolase(OPH)의 생산에 대하여 고찰하였다. OPH 생산의 향상을 위하여 성장 배지에 첨가되는 최적의 조건은 1.0 mM isopropyl-${\beta}$-D-thiogalactopytanoside (IPTG), 0.25 mM $Co^{2+}$ 및 0.1 mM ethylenediamine tetraacetate (EDTA) 이었다. 이 조건에서 최대OPH 생산은 $174Unit/L{\cdot}OD$를 나타내었다. 또한 1 mM의 Paraoxon은 OPH에 의하여 완전히 분해되었다. 이러한 연구 결과는 토양 및 수계에 잔류하는 환경독성 유기인 화합물을 제거하는 bioremediation의 수수단으로 활용될 수 있음을 보여주었다.

• KSBB Journal
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• 제17권2호
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• pp.158-161
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• 2002

본 연구에서는 화학무기, 농약 등에 사용되는 신경독성물질인 유기인화합물의 측정을 위하여 유기인화합물의 효소반응 저해작용을 이용한 광바이오센서장치의 시제품을 제작하였다. 효소반응을 위하여 효소로는 신경세포의 필수효소인 acetylcholinesterase, acetylthiocholine iodide을 사용하였으며 효소반응의 저해제인 유기인화합물로는 paraoxon을 사용하였다. 센서의 폭정원리는 유기인화합물에 의해 저해된 효소반응정도를 효소반응의 생성물인 아세트산의 정량적 측정으로 분석하였으며, pH에 의하여 최대 흡광파장의 변화가 일어나는 litmus를 사용하여 흡광도 측정으로 아세트산의 정량분석을 수행하였다. 광바이오센서 시제품의 제작은 광원으로 고취도 LED와 광세기 측정을 위한 photodiode로 구성하였으며, 제작된 센서를 이용한 실험결과로부터 0 ppm에서 2 ppm의 paraoxon 농도에서 구성된 센서시스템의 선형적 신호 변화를 관찰하였다. 이상의 실헐결과로부터 광바이오센서 시제품은 2분의 반응시간으로 신속하고 정확한 유기인화합물의 정량분석이 가능함을 확인하였다.

• Bulletin of the Korean Chemical Society
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• 제31권6호
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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.