Proteinases inTrichomonas vaginalisandTritrichomonas mobilensisare not exclusively of cysteine type
- 1 February 1991
- journal article
- research article
- Published by Cambridge University Press (CUP) in Parasitology
- Vol. 102 (1) , 113-115
- https://doi.org/10.1017/s0031182000060418
Abstract
High molecular weight proteinases ofTrichomonas vaginalis(with apparentMrvalues 142 and > 220 kDa) andTritrichomonas mobilensis(Mr67, 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 inT. vaginalisand two proteinases inT. mobilensis(67 and 104 kDa) were inhibited by EDTA and EGTA suggesting that they belong to the metallo-proteinase class. The 67 kDa proteinase ofT. mobilensiswas inhibited also byo-phenanthroline. The other two bands ofT. 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.Keywords
This publication has 0 references indexed in Scilit: