曼氏血吸虫苹果酸脱氢酶的纯化、免疫化学及生物学特性研究

D. Bout, H. Dupas, M. Capron, A. El Gazawi , Y. Carlier, A. Delacourte , A. Capron
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引用次数: 16

摘要

利用AMP-Sepharose亲和层析技术纯化了曼氏血吸虫苹果酸脱氢酶,并对该酶的免疫化学和生物学特性进行了研究。MDH分子量为60000,具有两种同工酶(pI 7.1和8.5),它们的抗原性不同。同工酶(pI 7.1)是血吸虫特有的抗原,具有高度的免疫原性。通过免疫荧光法,MDH定位于盲肠的细胞层。用纯化的MDH免疫小鼠,虫负荷显著降低。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Purification, immunochemical and biological characterization of malate dehydrogenase ofSchistosoma mansoni

Affinity chromatography with AMP-Sepharose allows us to purify malate dehydrogenase ofSchistosoma mansoni and to perform the studies about the immunochemical and biological properties of this enzyme. MDH has a mol. wt 60,000 and has two isoenzymes (pI 7.1 and 8.5), which are antigenically different. Isoenzyme (pI 7.1) is the antigen called 4, specific of the genusSchistosoma and is highly immunogenic. By immunofluorescence, MDH was localized in the cellular layer of the coecum. Mice immunized with purified MDH exhibited a significant decrease of worm burden.

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