Bruchhaus I, Brattig N W, Tannich E
Bernhard Nocht Institute for Tropical Medicine, Hamburg, FR, Germany.
Arch Med Res. 1992;23(2):27-9.
A recombinant iron-containing superoxide dismutase (recFeSOD) of Entamoeba histolytica was produced in a prokaryotic expression system. Purified recFeSOD was found to be enzymatically active as determined by (i) inhibition of ferri-cytochrome c reduction, (ii) dismutation of superoxide anions generated by human neutrophils and (iii) inhibition of nitroblue tetrazolium reduction. The enzymatic properties of recFeSOD were similar to those of the native protein in trophozoite extracts. In an ELISA using recFeSOD as antigen, 96% of sera from patients having invasive amebiasis were reactive whereas none of the healthy controls or of patients suffering from malaria, bacterial or viral infections were reactive. Only sera of Toxoplasma-, Leishmania- or Trypanosoma-infected individuals exhibited partial cross-reactivity to recFeSOD.
溶组织内阿米巴的重组含铁超氧化物歧化酶（recFeSOD）在原核表达系统中产生。通过以下方法确定纯化的recFeSOD具有酶活性：（i）抑制铁细胞色素c还原；（ii）使人类中性粒细胞产生的超氧阴离子发生歧化反应；（iii）抑制氮蓝四唑还原。recFeSOD的酶学性质与滋养体提取物中天然蛋白的酶学性质相似。在以recFeSOD作为抗原的ELISA检测中，96%的侵袭性阿米巴病患者血清呈反应性，而健康对照者以及疟疾、细菌或病毒感染患者的血清均无反应性。仅弓形虫、利什曼原虫或锥虫感染个体的血清对recFeSOD表现出部分交叉反应性。
Zotero 插件