title: Purification of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi by affinity chromatography.
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.
authors.affiliation: Instituto de Investigaciones Bioquímicas Luis F. Leloir, Fundación Campomar, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, CONICET, Argentina.
authors.forename: C
authors.initials: C
authors.lastname: Labriola
authors.forename: M
authors.initials: M
authors.lastname: Sousa
authors.forename: J J
authors.initials: JJ
authors.lastname: Cazzulo
mesh_terms: D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods; D003208:Concanavalin A; D015891:Cystatins; D003546:Cysteine Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D015800:Protozoan Proteins; D012685:Sepharose; D014349:Trypanosoma cruzi / Q000201:enzymology*
chemical_list: D015891:Cystatins; D015800:Protozoan Proteins; D003208:Concanavalin A; D012685:Sepharose; D003546:Cysteine Endopeptidases; C063214:cruzipain