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首页> 外文期刊>Infection and immunity >Identification and purification of a second form of Cu/Zn superoxide dismutase from Schistosoma mansoni.
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Identification and purification of a second form of Cu/Zn superoxide dismutase from Schistosoma mansoni.

机译：鉴定和纯化曼氏血吸虫的第二种形式的Cu / Zn超氧化物歧化酶。

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Our laboratories previously isolated a putative extracellular or membrane-associated Cu/Zn superoxide dismutase (Cu/Zn-SOD) gene, designated a signal peptide-containing (SP) Cu/Zn-SOD, from Schistosoma mansoni. SOD activity was thus investigated throughout the life cycle of S. mansoni and found in all stages: eggs, miracidia, cercariae, schistosomula, lung-stage worms, and adult worms. The adult worms had the highest SOD activity (53 +/- 9 nitrite units), which was five times higher than that of eggs or miracidia and twice as high as that of 3-h-old mechanically transformed schistosomula. Cu/Zn-SOD constituted over 95% of the total SOD activity found in S. mansoni, compared with that of Mn-SOD. Most of Cu/Zn-SOD specific activity was associated with a detergent-extractable fraction of the parasite. Isoelectric focusing gel electrophoresis analysis revealed that there were four major pI variants of Cu/Zn-SOD present in the adult worms. Only two of these Cu/Zn-SOD pI variants were present in the 3-h-old mechanically transformed schistosomula. Fast protein liquid chromatography gel filtration fractionation of adult parasite extract was carried out to correlate the SP Cu/Zn-SOD with the SOD activity by using anti-SP Cu/Zn-SOD monoclonal antibodies, which separated the immunoreactive gene product and the SOD activity into different fractions. Quantitative tissue fractionation also revealed a discordant distribution of the gene product compared with that of Cu/Zn-SOD activity. These results indicated the existence of another Cu/Zn-SOD(s) in the parasite. Purification of the Cu/Zn-SOD activity from the adult worms showed that it represented the two lower-pI variants found in both adult worms and 3-h-old schistosomula. Peptide sequence analysis of the purified Cu/Zn-SOD confirmed that there is a second form of Cu/Zn-SOD in the parasite.
机译：我们的实验室以前从曼氏血吸虫中分离出一种推定的细胞外或与膜相关的Cu / Zn超氧化物歧化酶（Cu / Zn-SOD）基因，该基因被命名为含信号肽（SP）的Cu / Zn-SOD。因此，在整个曼氏链球菌的整个生命周期中对SOD活性进行了研究，并发现了各个阶段的超氧化物歧化酶：卵，水母，尾c，血吸虫，肺蠕虫和成虫。成虫蠕虫的SOD活性最高（亚硝酸盐单位为53 +/- 9），是鸡蛋或水acid的5倍，是3小时大的机械转化血吸虫的2倍。与锰-SOD相比，Cu / Zn-SOD占曼氏酵母中总SOD活性的95％以上。 Cu / Zn-SOD的大多数比活性与寄生虫的去污剂可萃取级分有关。等电聚焦凝胶电泳分析表明，成虫中存在四种主要的Cu / Zn-SOD pI变体。这些铜/锌SOD pI变体中只有两个存在于3小时大的机械转化的血吸虫中。利用抗SP Cu / Zn-SOD单克隆抗体对成人寄生虫提取物进行快速蛋白质液相色谱凝胶过滤分离，以将SP Cu / Zn-SOD与SOD活性相关，从而分离了免疫反应性基因产物和SOD活性分成不同的部分。定量组织分级还显示与Cu / Zn-SOD活性相比，基因产物分布不一致。这些结果表明该寄生虫中存在另一种Cu / Zn-SOD。从成虫中纯化Cu / Zn-SOD活性表明，它代表了在成虫和3小时大的血吸虫中发现的两个较低的pI变体。纯化的Cu / Zn-SOD的肽序列分析证实，该寄生虫中存在第二种形式的Cu / Zn-SOD。

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