Digestion of human immunoglobulin G by the major cysteine proteinase (cruzipain) from Trypanosoma cruzi
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 extens...
Guardado en:
| Autor principal: | |
|---|---|
| Publicado: |
1990
|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03781097_v70_n3_p337_Bontempi http://hdl.handle.net/20.500.12110/paper_03781097_v70_n3_p337_Bontempi |
| Aporte de: |
| Sumario: | 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. © 1990 Federation of European Microbiological Societies. |
|---|