title: Purification and partial characterization of a cysteine proteinase from Trypanosoma rangeli.
abstract: 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 Cystatin-Sepharose. This CP had a similar apparent molecular mass and an identical 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-phenanthroline or Pepstatin, and was able to use the same substrates, although with different order of effectiveness and optimum pH.
authors.affiliation: Instituto de Investigaciones Bioquímicas, Fundación Campomar, Buenos Aires, Argentina.
authors.forename: C
authors.initials: C
authors.lastname: Labriola
authors.forename: J J
authors.initials: JJ
authors.lastname: Cazzulo
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification*; D004789:Enzyme Activation; D008969:Molecular Sequence Data; D013379:Substrate Specificity; D014345:Trypanosoma / Q000201:enzymology*
chemical_list: D003546:Cysteine Endopeptidases