title: Digestion of human immunoglobulin G by the major cysteine proteinase (cruzipain) from Trypanosoma cruzi.
abstract: The major cysteine proteinase (cruzipain) from Trypanosoma cruzi was able to digest human IgG, as shown by polyacrylamide gel electrophoresis in the presence of SDS, and by gel filtration on a Superose 12 column, in a FPLC system. The Fab fragment of IgG was only slightly degraded, but Fc was extensively hydrolyzed to small peptides. The results suggest that cruzipain might be involved in the defense mechanisms of the parasite against the immune response of the host.
authors.affiliation: Instituto Nacional de Diagnóstico e Investigación de la Enfermedad de Chagas Dr. Mario Fatala Chaben, Misteria de Salud y Acción Social, Buenos Aires, Argentina.
authors.forename: E
authors.initials: E
authors.lastname: Bontempi
authors.forename: J J
authors.initials: JJ
authors.lastname: Cazzulo
mesh_terms: D000818:Animals; D003546:Cysteine Endopeptidases; D006801:Humans; D006868:Hydrolysis; D007140:Immunoglobulin Fab Fragments; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D015800:Protozoan Proteins; D014349:Trypanosoma cruzi / Q000201:enzymology*
chemical_list: D007140:Immunoglobulin Fab Fragments; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D015800:Protozoan Proteins; D003546:Cysteine Endopeptidases; C063214:cruzipain