Purification of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi by affinity chromatography

Biol Res. 1993;26(1-2):101-7.

Abstract

The major cysteine proteinase from Trypanosoma cruzi, cruzipain, can be obtained essentially homogeneous, starting from crude epimastigote extracts, in one step, by affinity chromatography on Cystatin-Sepharose (specific for cysteine proteinases) or ConA-Sepharose (specific for high mannose N-linked glycoproteins). The methods offer considerable potential for enzyme purification from scarce sources, such as other parasite stages or radioactively labelled material with high specific radioactivity.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chromatography, Affinity / methods
  • Concanavalin A
  • Cystatins
  • Cysteine Endopeptidases / isolation & purification*
  • Cysteine Endopeptidases / metabolism
  • Protozoan Proteins
  • Sepharose
  • Trypanosoma cruzi / enzymology*

Substances

  • Cystatins
  • Protozoan Proteins
  • Concanavalin A
  • Sepharose
  • Cysteine Endopeptidases
  • cruzipain