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Characterization of a purified proteinase from Trichomonas vaginalis was carried out using bacitracin-sepharose affinity chromatography. Trichomonas vaginalis KT-9 isolate was used as a source of enzyme study. Proteinase activity was determined using Bz-Pro-Phe-Arg-Nan as the substrate. Optimum pH for the purified proteinase activity was 7.0 and 6.0, 9.0 with DTT. Optimum temperature was 37 degrees C and isoelectric point was 7.2. Activity of this proteinase was inhibited by E-64, antipain, leupeptin, Hg2+ and Zn2+ and activated by DTT and cysteine. Activity of the purified proteinase was visualized by gelatin SDS-PAGE. The gelatinolytic activity of the purified proteinase was inhibited by E-64, antipain, leupeptin, and IAA, but not by PMSF and EDTA. On SDS-PAGE, the molecular weight of the purified proteinase was 60,000 daltons. Sera of rabbits infected with T. vaginalis reacted specifically in immunoblots with this proteinase. These results indicate that 60 kDa of purified proteinase was cysteine proteinase with antigenicity.
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