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Proteinases in Trichomonas vaginalis and Tritrichomonas mobilensis are not exclusively of cysteine type

Published online by Cambridge University Press:  06 April 2009

P. Bózner  and
P. Demeš
P. Bózner
Affiliation:
Department of Microbiology and Immunology, Medical Faculty, Comenius University, Sasinkova 4, 811 08 Bratislava, Czechoslovakia
P. Demeš
Affiliation:
Institute of Immunology, Comenius University, Sasinkova 4, 811 08 Bratislava, Czechoslovakia
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Summary

High molecular weight proteinases of Trichomonas vaginalis (with apparent Mr values 142 and > 220 kDa) and Tritrichomonas mobilensis (Mr 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.

Keywords

Trichomonas vaginalisTritrichomonas mobilensisproteinasesmetallo-proteinases
Type
Research Article
Information
Parasitology , Volume 102 , Issue 1 , February 1991 , pp. 113 - 115
Copyright
Copyright © Cambridge University Press 1991

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