采用自身配对设计,对16例胃癌组织GGT 及其同工酶进行生化研究。定量检测表明癌组织内GGT 异常升高,其比活性(U/g 蛋白)与远癌组织(对照组)的差异有非常显著性意义(t=5.55,P<0.01)。组织GGT 呈现多区带变化,胃癌组织GGT 同工酶表现为原位活性明显增强,小分子同工酶区带(Ⅰ、Ⅱ)出现多,快速泳动的GGT-Ⅰ出现率较远癌组高(P<0.025)。酶组化证实远癌组GGT 为阴性,而癌组织大多可见GGT 阳性物质,提示GGT 是胃癌标志酶之一。 A paired design was used to biochemically study GGT and its isozymes in 16 cases of gastric cancer. Quantitative detection showed abnormal increase of GGT in cancer tissues, and the difference between specific activity (U/g protein) and distant cancer tissue (control group) was very significant (t=5.55, P<0.01). The organization GGT showed multi-zone changes. The GGT isoenzymes in gastric cancer tissues showed a significant increase in in situ activity, with a large number of small molecule isoenzyme bands (I, II), and a higher rate of rapid GGT-I migration than that of distant cancer tissues. High (P<0.025). Enzymatic histochemistry confirmed that GGT was negative in the distal cancer group, and GGT positive substances were mostly found in cancer tissues, suggesting that GGT is one of the gastric cancer marker enzymes.