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从人胎盘中分离得到谷胱甘肽S-转移酶纯化倍数470倍.比活力为37.897μmol/min·mg.经PAGE和SDS-PAGE证实为一条区带,亚基分子量为23000 Dalton;等电聚焦电泳结果,此酶等电点为4.6.底物GSH和CDNB的Km值分别为0.259mmol/L(r=0.97)和0.350mmol/L(r=0.99).不同浓度的巯基乙醇对GST-π活性有保护作用,1mmol/L浓度的保护作用较强.DEN,Triton X—100、苯巴比妥钠和AAF对GST-π活性起抑制作用,抑制作用随浓度增高而加强.
The purity of glutathione S-transferase was 470-fold and the specific activity was 37.897μmol / min · mg from human placenta.It was confirmed as a band by PAGE and SDS-PAGE, the molecular weight of subunit was 23000 Dalton, Focusing on the results of electrophoresis, the isoelectric point of this enzyme was 4.6.The Km values of GSH and CDNB were 0.259mmol / L (r = 0.97) and 0.350mmol / L (r = 0.99) respectively.The effect of different concentrations of mercaptoethanol on GST- π activity, the protective effect of 1mmol / L concentration was stronger.DEN, Triton X-100, phenobarbital and AAF inhibited the activity of GST-π, and the inhibitory effect was enhanced with the increase of concentration.