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NIGG H. N.; RAMOS L. E.; GRAHAM E. M.; STERLING J.; BROWN S.; CORNELL J. A. 《Toxicological sciences》1996,33(2):272-281
The purpose of these experiments was to determine the reversibilityof -chaconine and -solanine inhibition of human plasma butyrylcholinesterase(BuChE). For the substrate -naphthylacetate, optimal assay conditionswere 0.50 M sodium phosphate buffer and a substrate concentrationof 35 ' 104 M. Dibucaine (1 ' 105 M) indicatedthe usual phenotype for all subjects; -chaconine and -solanineat 2.88 ' 106 M inhibited BuChE about 70 and 50%, respectively.One-and 24-hr incubations at 1 ' 101 M with -chaconine,-solanine, paraoxon, eserine, and ethanol yielded reversibleinhibition with dilution except for paraoxon. Twenty-four-hourdialyses of incubations showed no inhibition except for paraoxon.PAGE enzyme activity gels of 1-and 24-hr incubations also showedno inhibition except for paraoxon. -Chaconine and -solanineare reversible inhibitors of human butyrylcholinesterase. Atestimated tissue levels, -chaconine, -solanine, and solanidineinhibited BuChE 1086%. In assays which combined -chaconine,-solanine, and solanidine, inhibition of BuChE was less thanadditive. No inhibition of albumin -naphthylacetate esterase(an arylesterase) was noted with any inhibitor. The importanceof these data to adverse toxicological effects of potato alkaloidsis discussed. 相似文献
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