中文摘要：

从 Liposcelis bostrychophila Badonnel 和 L 的谷胱甘肽 S-transferases (GST ) 。entomophila (Enderlein )(Psocoptera：Liposcelididae ) 被 glutathione-agarose 亲密关系层析净化，并且向人工的底层 1-chloro-2,4-dinitrobenzene (CDNB ) 由他们的 Michaelis-Menten 动力学随后描绘了并且分别地减少了谷胱甘肽(GSH ) 。向 CDNB 的净化的 GST 的特定的活动在 L 更高是 2.3 褶层。bostrychophila 比在 L。entomophila。尽管净化的酶的特定的活动在二种之间变化了，纯化收益是类似的。SDS 页为两个在 23 kDa 揭示了一个乐队种类。L 的 GST。entomophila 展出了更高的 Michaelis-Menten 常数(Km ) 但是更低的最大的速度(Vmax ) 价值比那些 L。bostrychophila。为 L 的 CDNB 变化形式的最佳 pH。bostrychophila 和 L。entomophila GST 是 7.0 和 7.5，并且最佳温度分别地是 35 和 40 掳 C。抑制动力学证明 cibacron 蓝色， curcumin， bromosulfalein， ethacrynic 酸，和 carbosulfan 在种类，而是 beta-cypermethrin， fenpropathrin， tetraethylthiuram 二硫化物，和 diethyl maleate 的禁止的效果在 GST 上有优秀禁止的效果不是重要的。

英文摘要：

Glutathione S-transferases（GSTs） from Liposcelis bostrychophila Badonnel and L.entomophila（Enderlein）（Psocoptera：Liposcelididae） were purified by glutathione-agarose affinity chromatography,and characterized subsequently by their Michaelis-Menten kinetics toward the artificial substrates 1-chloro-2,4-dinitrobenzene（CDNB） and reduced glutathione（GSH）,respectively.The specific activity of the purified GST toward CDNB was 2.3-fold higher in L.bostrychophila than in L.entomophila.Though the specific activities of purified enzymes varied between the two species,the purification yields were similar.SDS-PAGE revealed one band at 23 kDa for both the species.GSTs of L.entomophila exhibited higher Michaelis-Menten constants（Km） but lower maximal velocity（Vmax） values than those of L.bostrychophila.The optimum pH for CDNB conjugation of L.bostrychophila and L.entomophila GSTs was 7.0 and 7.5,and optimum temperature was 35 and 40°C,respectively.Inhibition kinetics showed that cibacron blue,curcumin,bromosulfalein,ethacrynic acid,and carbosulfan had excellent inhibitory effects on GSTs in both species,but the inhibitory effects of beta-cypermethrin,fenpropathrin,tetraethylthiuram disulfide,and diethyl maleate were not significant.