PROTEINASES IN TRICHOMONAS-VAGINALIS AND TRITRICHOMONAS-MOBILENSIS ARE NOT EXCLUSIVELY OF CYSTEINE TYPE

被引:25
作者
BOZNER, P [1 ]
DEMES, P [1 ]
机构
[1] COMENIUS UNIV,INST IMMUNOL,CS-81108 BRATISLAVA,CZECHOSLOVAKIA
关键词
TRICHOMONAS-VAGINALIS; TRITRICHOMONAS-MOBILENSIS; PROTEINASES; METALLO-PROTEINASES;
D O I
10.1017/S0031182000060418
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
High molecular weight proteinases of Trichomonas vaginalis (with apparent M(r) values 142 and > 220 kDa) and Tritrichomonas mobilensis (M(r) 67, 86, 104 and 120 kDa), optimally active at pH 8, were analysed in gelatin-containing polyacrylamide gels. All of these proteinases were resistant to serine-, aspartic- as well as cysteine proteinase inhibitors. Both proteolytic bands in T. vaginalis and two proteinases in T. mobilensis (67 and 104 kDa) were inhibited by EDTA and EGTA suggesting that they belong to the metallo-proteinase class. The 67 kDa proteinase of T. mobilensis was inhibited also by o-phenanthroline. The other two bands of T. mobilensis (86, 120 kDa) were not classified to any proteinase group since they appeared to be resistant to the chelating agents tested in this study.
引用
收藏
页码:113 / 115
页数:3
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