Proteinases in Trichomonas vaginalis and Tritrichomonas mobilensis are not exclusively of cysteine type.
High molecular weight proteinases of Trichomonas vaginalis (with apparent Mr values 142 and greater than 220 kDa) and Tritrichomonas mobilensis (Mr 67, 86, 104 and 120 kDa), optimally active at pH8, 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.
Bózner
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Department of Microbiology and Immunology, Medical Faculty, Comenius University, Bratislava, Czechoslovakia.
Demes
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D000818:Animals; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D015853:Cysteine Proteinase Inhibitors; D004492:Edetic Acid / Q000494:pharmacology; D004533:Egtazic Acid / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010618:Phenanthrolines / Q000494:pharmacology; D011480:Protease Inhibitors / Q000494:pharmacology; D014246:Trichomonas vaginalis / Q000201:enzymology; D014318:Tritrichomonas / Q000201:enzymology*
D015853:Cysteine Proteinase Inhibitors; D010618:Phenanthrolines; D011480:Protease Inhibitors; D004533:Egtazic Acid; D004492:Edetic Acid; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D008666:Metalloendopeptidases; C025205:1,10-phenanthroline