PURIFICATION AND PARTIAL CHARACTERIZATION OF A CYSTEINE PROTEINASE FROM TRYPANOSOMA-RANGELI

Epimastigotes of the American Trypanosome Trypanosoma rangeli contain a very low cysteine proteinase (CP) activity. The enzyme was purified to homogeneity by affinity chromatography on ConA-Sepharose and Cystat in-Sepharose. This CP had a similar apparent molecular mass and an ide ntical N-terminal sequence (15 amino acids) as compared with cruzipain from Trypanosoma cruzi; cross-reacted immunologically with the latter enzyme, it was inhibited by E-64 and TLCK, but not by PMSF, o-phenant hroline or Pepstatin, and was able to use the same substrates, althoug h with different order of effectiveness and optimum pH.