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 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.
Labriola
C
C
Instituto de Investigaciones Bioquímicas, Fundación Campomar, Buenos Aires, Argentina.
Cazzulo
J J
JJ
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*
D003546:Cysteine Endopeptidases