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致病性溶组织内阿米巴96 kDa乙醇/乙醛脱氢酶(EhADH2)的表面定位、调控及生物学特性

Surface localization, regulation, and biologic properties of the 96-kDa alcohol/aldehyde dehydrogenase (EhADH2) of pathogenic Entamoeba histolytica.

作者信息

Flores B M, Stanley S L, Yong T S, Ali M, Yang W, Diedrich D L, Torian B E

机构信息

College of Pharmacy, Department of Pharmaceutical Sciences, Idaho State University, Pocatello 83209-8334, USA.

出版信息

J Infect Dis. 1996 Jan;173(1):226-31. doi: 10.1093/infdis/173.1.226.

Abstract

The 96-kDa surface antigen of Entamoeba histolytica was demonstrated through extensive immunologic evaluation with monoclonal and monospecific antibodies to be identical to or an isoform of the amebic alcohol/aldehyde dehydrogenase (EhADH2). EhADH2 was secreted, excreted, or shed into the culture medium in quantities commensurate with amebic growth when studied in a novel culture system. Of importance, using RNase protection assays, specific mRNA coding for the EhADH2 gene product(s) was up-regulated by treatment of viable trophozoites with the enzyme substrate ethanol. These data provide insight into the biology of this enzyme and its regulation by appropriate stressors.

摘要

通过使用单克隆抗体和单特异性抗体进行广泛的免疫学评估,证实溶组织内阿米巴的96-kDa表面抗原与阿米巴醇/醛脱氢酶(EhADH2)相同或为其同工型。在一个新型培养系统中进行研究时,EhADH2会以与阿米巴生长相称的量分泌、排泄或释放到培养基中。重要的是,使用核糖核酸酶保护试验,用酶底物乙醇处理活滋养体可使编码EhADH2基因产物的特异性mRNA上调。这些数据为该酶的生物学特性及其受适当应激源调控提供了深入了解。

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