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pubmed-article:2756715pubmed:abstractText1. Hydrolysis of the drug esters procaine, chloramphenicol succinate, and prednisolone succinate was studied. Addition of soman to guinea pig liver microsomes caused a dose-dependent inhibition of hydrolysis of all three substrates; at the highest soman concentration (1 microM), ester hydrolysis was totally abolished. 2. Ester hydrolysis was also measured in liver microsomes from guinea pigs pretreated with soman at a low dose (10% of LD50) or at a high dose (90% of LD50) either 1 h or 12 h before killing. Plasma-cholinesterase activity was decreased in all pretreated animals. Liver carboxylesterase activity, measured with the three drug substrates and by hydrolysis of 4-nitrophenyl acetate was increased by all pretreatments. 3. This enhancing effect varies with the substrate and increases with dose of soman. The 12 h pretreatment produced a greater increase in activity than did the 1 h pretreatment. 4. These studies indicate that soman is a potent inhibitor of carboxylesterase activity in vitro but increases the activity of the liver enzyme when administered in vivo.lld:pubmed
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pubmed-article:2756715pubmed:pagination115-21lld:pubmed
pubmed-article:2756715pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:2756715pubmed:year1989lld:pubmed
pubmed-article:2756715pubmed:articleTitleAlteration of hepatic carboxylesterase activity by soman: inhibition in vitro and enhancement in vivo.lld:pubmed
pubmed-article:2756715pubmed:affiliationDepartment of Pharmacology, Eastern Virginia Medical School, Norfolk 23501.lld:pubmed
pubmed-article:2756715pubmed:publicationTypeJournal Articlelld:pubmed
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pubmed-article:2756715pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed