Open AccessDigestion of human immunoglobulin G by the major cysteine proteinase (cruzipain) from Trypanosoma cruzi
Author(s) -
Bontempi Esteban,
Cazzulo Juan José
Publication year - 1990
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1990.tb14000.x
Subject(s) - trypanosoma cruzi , fast protein liquid chromatography , biochemistry , polyacrylamide gel electrophoresis , antibody , biology , cysteine , gel electrophoresis , immunoglobulin fc fragments , immune system , immunoglobulin g , chemistry , parasite hosting , enzyme , immunology , world wide web , computer science
1. Summary 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.