幽门螺杆菌尿素酶抗原的分离及纯化

The Purification of Helicobacter Pylori Urease

本实验采用新型离子交换剂SourceQ15为分离介质 ,用氯化钠盐浓度梯度洗脱法 ,从幽门螺杆菌超声处理上清液中纯化了幽门螺杆菌尿素酶抗原 ,所得纯化物经SDS PAGE电泳分析证明具有良好的纯度 ,只含有分子量为 6 6 0 0 0及 2 95 0 0两种蛋白成分 ,与幽门螺杆菌两种亚基的大小完全相同。以此纯化尿素酶为抗原用于ELISA检测临床确诊的幽门螺杆菌感染者血清 12例及未感染幽门螺杆菌者血清 18例 ,其ELISA阳性及阴性符合率达到10 0 %。提示本法纯化的幽门螺杆菌尿素酶抗原用于ELISA检测幽门螺杆菌感染者血清抗体具有良好的前景。

The Helicobacter Pylori urease was purified by the new type ion-exchanger Source Q15.Only two protein bands was shown at 66 kD and 29.5 kD by SDS-PAGE.This purified urease had been used as the ELISA coating antigen to detect 12 serum specimens from the patients infected with H.Pylori and 18 normal serum samples.The 12 patient serum specimens gave positive results and the 18 normal serum samples were nagetive in the ELISA.