Purification of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi by affinity chromatography.
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.
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Instituto de Investigaciones Bioquímicas Luis F. Leloir, Fundación Campomar, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, CONICET, Argentina.
Sousa
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Cazzulo
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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*
D015891:Cystatins; D015800:Protozoan Proteins; D003208:Concanavalin A; D012685:Sepharose; D003546:Cysteine Endopeptidases; C063214:cruzipain