摘要
本文采用超凝胶柱层析法分离纯化日本血吸虫成虫31/32KD抗原。分离的抗原经银染色及免疫印迹法分析证明已达免疫纯及生化纯级。该抗原PAS染色呈阴性,经过碘酸钠处理后不失去活性,在琼脂糖凝胶电泳中趋向阳极。鉴于血吸虫成虫31/32KD组分是一种主要血清学抗原,它的分离纯化为改进和标化血吸虫病的诊断提供了条件。
After AcA54 Ultra-gel column chromatography the soluble antigen from Schistosoma japonicum adult worm produced 4 peaks of proteins. Serologic antigenic activities were seen in the first to the third peak as detected by ELISA. The antigen isolated by ultragel chromatography was further purified by dialysis, precipitation and high-speed centrifugation. The purity of the purified fraction was confirmed by silver staining as a 31/32KD protein after SDS-PAGE. This antigen moves towards anode during electrophoresis in agarose gel, which can not be stained by PAS. After treated with pe-riodate it still can be binded by corresponding antibodies. Therefore it is assumed that S. Japonicum adult worm protein isolated and purified in this work is the similar antigen as S. mansoni 31/32KD diagnostic protein or S. mansoni hemoglobinase previously reported.
出处
《湖南医科大学学报》
CSCD
1990年第4期307-311,共5页
Bulletin of Hunan Medical University
基金
TDR/WHO资助课题
关键词
日本血吸虫
抗原
免疫化学
Schistosoma japonicum
antigen
31/32KD adult worm antigen
isola- tion and purification
immunochemistry
diagnostic use
