Functional properties of hemocyanin from Oncomelania hupensis, the intermediate host of Schistosoma japonicum

被引：18

作者：

Guo, Daoyi ^{[1
]}

Zhang, Yun ^{[1
]}

Zeng, Dan ^{[1
]}

Wang, Hua ^{[1
]}

Li, Xun ^{[1
]}

Li, Yongdong ^{[1
]}

Fan, Xiaolin ^{[1
]}

机构：

[1] Gannan Normal Univ, Key Lab Organopharmaceut Chem, Ganzhou 341000, Jiangxi, Peoples R China

来源：

EXPERIMENTAL PARASITOLOGY | 2009年 / 123卷 / 03期

基金：

美国国家科学基金会;

关键词：

Oncomelania hupensis; Hemocyanin; o-Diphenoloxidase; Carbohydrate epitopes; Schistosoma japonicum; AMINO-ACID-SEQUENCE; PHENOLOXIDASE ACTIVITY; RAPANA-THOMASIANA; N-GLYCANS; STRUCTURAL-CHARACTERIZATION; BIOMPHALARIA-GLABRATA; MOLLUSCAN HEMOCYANIN; HALIOTIS-TUBERCULATA; CROSS-REACTIVITY; MANSONI;

D O I：

10.1016/j.exppara.2009.07.013

中图分类号：

R38 [医学寄生虫学]; Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ; 100103 ;

摘要：

The gastropod mollusc, Oncomelania hupensis is a unique intermediate host for the human parasite Schistosoma japonicum. It is a primary factor for the epidemic of schistosomiasis and its distribution is consistent with the epidemic area of schistosomiasis. Here we report the functional properties of hemocyanin of O. hupensis (OhH), a copper-containing respiratory protein which was isolated from its hemolymph and purified by ammonium sulfate fractionation and ultracentrifugation. We identified the protein characters including UV absorption at 340 nm, copper content and quaternary structure. Furthermore, by induction of phenoloxidase and enzyme-linked immunosorbent assay we show that OhH exhibited o-diphenoloxidase activity after limited proteolysis, and shared carbohydrate epitopes with glycoconjugates of S. japonicum. (C) 2009 Elsevier Inc. All rights reserved.

引用

页码：277 / 281

页数：5

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