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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。
In this experiment, a new type of ion exchanger SourceQ15 was used as the separation medium, and the H. pylori urease antigen was purified from the H. pylori supernatant by sodium chloride salt concentration gradient elution. The purified product was analyzed by SDS PAGE Proved to have good purity, only contains a molecular weight of 6 6 0 0 0 and 2 95 0 0 two protein components, and Helicobacter pylori two subunits of the same size. The purified urease was used as an antigen in ELISA to detect 12 serum samples of clinically confirmed Helicobacter pylori and 18 samples of non-infected H. pylori, and the coincidence rate of ELISA positive and negative was 100%. It is suggested that the purified H. pylori urease antigen of the present method has good prospects for ELISA for detecting serum antibodies against Helicobacter pylori infection.