Toxoplasma gondii:: Purification and characterization of an immunogenic metallopeptidase

被引：16

作者：

Berthonneau, J ^{[1
]}

Rodier, MH ^{[1
]}

El Moudni, B ^{[1
]}

Jacquemin, JL ^{[1
]}

机构：

[1] CHU La Miletrie, Lab Parasitol & Mycol Med, Unite Rech Biol Parasitaire, F-86021 Poitiers, France

来源：

EXPERIMENTAL PARASITOLOGY | 2000年 / 95卷 / 02期

关键词：

Toxoplasma gondii; aminopeptidase; invasion; apicomplexa;

D O I：

10.1006/expr.2000.4524

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：

A Toxoplasma gondii aminopeptidase specific for the fluorogenic substrate L-arginine 7-amino-4-methylcoumarin was identified in cell-free extract. This enzyme was purified by high-performance liquid chromatography using first size exclusion, then anion exchange, followed by a second size exclusion. The purified enzyme exhibited a pI of 4.7 by chromatofocusing and had an apparent molecular weight of 110 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions. The purification factor was 80.9 and the yield was 14%. The optimal activity was at pH 7.4 and was strongly inhibited by EDTA and o-phenanthroline. Antibodies against this T. gondii metallopeptidase were detected by immunoprecipitation and immunoblotting in human sera obtained from patients under-going toxoplasmosis.(C) 2000 Academic Press.

引用

页码：158 / 162

页数：5

共 25 条

[1] A subtilisin-like protein in secretory organelles of Plasmodium falciparum merozoites [J].