Identity of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi and an antigen (Ag163B6) isolated with a monoclonal antibody

Cruzipain, purified by conventional methods, and Ag163B6, isolated by affinity chromatography with a monoclonal antibody raised against a T. cruzi extract, are glycoproteins with a similar electrophoretic mobility, which reacted with sera from most chronic chagasic patients. Their behaviour in SDS-P...

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Veröffentlicht in:	Immunology letters 1993, Vol.35 (1), p.59-62
Hauptverfasser:	Malchiodi, E.L., Chiaramonte, M.G., Martinez, J.A., Zwirner, N.W., Margni, R.A., Cazzulo, J.J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Ag163B6 Animals Antibodies, Monoclonal Antigens, Protozoan - chemistry Antigens, Protozoan - isolation & purification Blotting, Western Cruzipain Cysteine Endopeptidases - chemistry Cysteine Endopeptidases - immunology Cysteine Endopeptidases - isolation & purification Electrophoresis, Gel, Two-Dimensional Immunodiffusion Isoelectric Focusing Protozoan Proteins Trypanosoma cruzi - enzymology Trypanosoma cruzi - immunology
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Beschreibung
Zusammenfassung:	Cruzipain, purified by conventional methods, and Ag163B6, isolated by affinity chromatography with a monoclonal antibody raised against a T. cruzi extract, are glycoproteins with a similar electrophoretic mobility, which reacted with sera from most chronic chagasic patients. Their behaviour in SDS-PAGE, Western blotting, isoelectric focusing, two-dimensional electrophoresis (IEF and SDS-PAGE), Ouchterlony's double diffusion, and enzyme activity in SDS-PAGE gels containing 0.1% gelatin suggests that they are identical.
ISSN:	0165-2478 1879-0542
DOI:	10.1016/0165-2478(93)90148-U