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Phosalone 의 활성화과정을 통한 acetylcholinesterase 와 butyrylcholinesterase 에 대한 활성 저해
임금춘(Geum Choon Lim),허장현(Jang Hyun Hur),한대성(Dae Sung Han) 한국응용생명화학회 1995 Applied Biological Chemistry (Appl Biol Chem) Vol.38 No.2
The purpose of this study was to investigate a role of cytochrome P_(450), for the toxicity of the phosalone in in vitro and in vivo bioactivation systems. The bimolecular inhibition rate constants(k_i) of the phosalone to acetylcholinesterase(AChE) and butyrylcholinesterase(BuChE) were approximately 10²M^(-1)min^(-1), respectively, which meant a poor inhibitor. The potency of the phosalone as an inhibitor of AChE and BuChE was increased about 300 and 40 fold, respectively, when the inhibitor and the ChE were incubated with microsomes fortified with NADPH compared with microsome alone. Piperonyl butoxide(PB) addition to these coupled systems greatly reduced the inhibition of both target enzymes by blocking a bioactivation process. The I_(50), value of the Phosalone alone for rat brain AChE was 170 ㎎/㎏. When PB was pretreated, that value was altered to 42.5 ㎎/㎏. PB pretreatment synergized the inhibition of brain AChE with four times. Rat blood erythrocyte AChE and plasma BuChE were similarly inhibited in vivo by the phosalone and PB pretreatment didn`t affect significantly the pattern of the inhibition. The in vivo studies showed different results in the role of cytochrome P_(450) from those of the in vitro studies.
유기인계 살충제 Phosalone 원제 중의 불순물 동정 및 독성효과
임금춘,허장현,한대성 한국환경농학회 1995 한국환경농학회지 Vol.14 No.2
The purpose of this study was to investigate the identification and the toxicological effects of some impurities present in the technical grade phosalone (94.4%). In instrumental analyses of the technical phosalone, the five impurities such as phosalone oxon, 6-chloro-3-methylthio-2-oxobenzoxazole, 6-chloro-2-oxobenzoxazole, O,O,S-triethyl phosphorodithioate (OOSTEPDT) and dichlorophosalone were identified. The bimolecular inhibition rate constants (k_i) indicated that the technical phosalone inhibited both AChE and BuChE about ten times faster than the purified phosalone did. From in vivo studies the technical phosalone showed greater inhibition for mouse brain AChE, rat blood ChE's and mouse cytosolic non-specific esterases. It was presumed that some impurities present in the technical phosalone such as phosalone oxon cause such inhibition patterns of the technical phosalone observed in this study.