首页 | 本学科首页   官方微博 | 高级检索  
     

日本血吸虫成虫31/32KD抗原的纯化及其免疫化学特性
引用本文:汪世平,易新元,曾宪芳. 日本血吸虫成虫31/32KD抗原的纯化及其免疫化学特性[J]. 中南大学学报(医学版), 1990, 0(4)
作者姓名:汪世平  易新元  曾宪芳
作者单位:湖南医科大学寄生虫学教研室 研究生(汪世平),湖南医科大学寄生虫学教研室 导师(易新元),湖南医科大学寄生虫学教研室 导师(曾宪芳)
基金项目:TDR/WHO资助课题
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。

关 键 词:日本血吸虫  抗原  虫卵可溶性抗原~*  成虫31/32KD抗原~*  分离与提纯  免疫化学

PURIFICATION AND CHARACTERIZATION OF 31/32KD ANTIGEN FROM SCHISTOSOMA JAPONICUM ADULT WORMS
Wang Sniping Yi Xinyuan Zeng Xianfang. PURIFICATION AND CHARACTERIZATION OF 31/32KD ANTIGEN FROM SCHISTOSOMA JAPONICUM ADULT WORMS[J]. Journal of Central South University. Medical sciences, 1990, 0(4)
Authors:Wang Sniping Yi Xinyuan Zeng Xianfang
Affiliation:Wang Sniping Yi Xinyuan Zeng XianfangDepartment of Parasitoiogy,Hunan Medical University
Abstract: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.
Keywords:Schistosoma japonicum  antigen  31/32KD adult worm antigen  isola- tion and purification  immunochemistry  diagnostic use
本文献已被 CNKI 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号