Biochemical properties of purified cathepsin B from Schistosoma mansoni

被引：32

作者：

Ghoneim, H ^{[1
]}

Klinkert, MQ ^{[1
]}

机构：

[1] CNR,IST BIOL CELLULARE,I-00137 ROME,ITALY

来源：

INTERNATIONAL JOURNAL FOR PARASITOLOGY | 1995年 / 25卷 / 12期

关键词：

Schistosoma mansoni; cysteine proteinase; cathepsin B; purification;

D O I：

10.1016/0020-7519(95)00079-8

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 previously described ''major acidic proteinase'' of adult Schistosoma mansoni, believed to play a key role in the parasite's metabolism, has been identified as a cathepsin B (Sm31). Purified Sm cathepsin B was not recognized by anti-Sm32 or anti-cathepsin L antibodies. The enzyme hydrolyzes the synthetic protease substrates Z-Arg-Arg-AMC and Z-Phe-Arg-AMC as well as protein substrates. Its pH optimum is 3.0 with serum albumin, 4.0-5.0 with globin and 5.5-6.0 with the synthetic substrates. The enzyme was inactivated by cysteine proteinase inhibitors. Its activity against protein substrates would support the hypothesis that it plays a role in schistosome nutrition.

引用

页码：1515 / 1519

页数：5

共 12 条

[1]

BARRETT AJ, 1981, METHOD ENZYMOL, V80, P535

[2] SCHISTOSOMA-JAPONICUM - IMMUNOINHIBITORY STUDIES ON HEMOGLOBIN DIGESTION USING HETEROLOGOUS ANTISERUM TO BOVINE CATHEPSIN-D [J].