Purification and partial characterization of a cysteine proteinase from Trypanosoma rangeli

CARLOS LABRIOLA AND JUAN JOSÉ CAZZULO

FEMS MICROBIOLOGY LETTERS

WILEY-BLACKWELL PUBLISHING, INC

Lugar: England; Año: 1995 vol. 129 p. 143 - 148

0378-1097

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.