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A comparative study of the proteolytic enzymes of trypanosoma brucei trypanosoma equiperdum trypanosoma evansi trypanosoma vivax leishmania tarentolae and crithidia fasciculata



A comparative study of the proteolytic enzymes of trypanosoma brucei trypanosoma equiperdum trypanosoma evansi trypanosoma vivax leishmania tarentolae and crithidia fasciculata



Molecular & Biochemical Parasitology 9(2): 161-180



Four types of proteolytic activity were detected in the bloodstream form each of the 4 Trypanosoma species: [hide powder azure] HPAase, active on hide powder azure and detected on polyacrylamide gels containing denatured hemoglobin; [azocasein] AZCase, active on azocasein; type 1, active on the chromogenic peptide N-benzoyl-L-prolyl-L-phenylalanyl-L-arginine p-nitroanilide in the presence of dithiothreitol, and type 2, active against several nitroanilide derivatives in the absence of dithiothreitol. Studies of the pH optimum, dithiothreitol reqirement and inhibitor sensitivities of the proteolytic activities suggest that: HPAase and type 1 activities could be due to the same enzymes, probably a family of cysteine proteinases; AZCase had some characteristics of a cysteine proteinase, but was not identical to HPAase, and type 2 activity could be due to a serine proteinase. Procyclic T. brucei [from infected mouse blood] contained relatively low cysteine proteinase activities (HPAase, AZCase and type 1) but high type 2 activity. Their proteolytic enzymes were apparently more similar to those in C. fasciculata and L. tarentolae promastigotes than those in T. brucei bloodstream forms.

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