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Procarbamate계 살충제 benfuracarb의 산화적 활성화 과정을 통한 독성발현
유용만(Yong-Man Yu),김은향(Eun H. Kim),김성문(Songmun Kim),허장현(Jang-Hyun Hur) 한국농약과학회 2003 농약과학회지 Vol.7 No.1
This study was conducted to understand the role of oxidative enzyme cytochrome P₄?? in the bioactivation of benfuracarb and to know metabolites of benfuracarb by cytochrome P₄??. The bimolecular inhibition rate constant (k<SUB>i</SUB>) of benfuracarb on acetylcholinesterase (AChE) was as low as 1.1×10³ M?¹ min?¹, suggesting that benfuracarb should be activated for its toxic action. The potency of benfuracarb on AChE in the oxidase system (cytochrome P₄?? + NADPH) in vitro was 10-fold higher than that of control (cytochrome P₄??). Such a similar result was also found in the oxidase + PBO system. In vivo the I?? of benfuracarb was 22.7 ㎎ ㎏?¹, but pie-treatment of piperonyl butoxide (PBO) reduced the I?? by>100 ㎎ ㎏?¹, This result suggests that cytochrome P4S0 was involved in the activation of benfuracarb. Using microsomal oxidase system, metabolites of benfuracarb were elucidated. Fifty-eight percent of benfuracarb was converted to carbofuran, a major toxic metabolite, in the oxidase system, while only less than two percent of benfuracarb was converted to carbofuran in the oxidase + PBO system. These results also suggest that cytochrome P₄?? was involved in the activation of benfuracarb. Overall results indicate that cytochrome P₄?? could be involved in the bioactivation of benfuracarb to carbofuran.