Specific cleavage sites on human IgG subclasses by cruzipain, the major cysteine proteinase from Trypanosoma cruzi
P Berasain, C Carmona, B Frangione… - Molecular and …, 2003 - Elsevier
Cruzipain, the major cysteine proteinase of Trypanosoma cruzi, might have other biological
roles than its metabolic functions. In this report, we have explored the interaction of cruzipain
with molecules of the immune system. The enzyme was used to digest all human IgG
subclasses at different pH values and lengths of time. At pH 7.3, all subclasses were readily
split at the hinge region. Immunoblot and amino acid sequence analysis showed fragments
of IgG1 and IgG3 to be compatible with Fab and Fc, whereas IgG2 and IgG4 rendered Fab2 …
roles than its metabolic functions. In this report, we have explored the interaction of cruzipain
with molecules of the immune system. The enzyme was used to digest all human IgG
subclasses at different pH values and lengths of time. At pH 7.3, all subclasses were readily
split at the hinge region. Immunoblot and amino acid sequence analysis showed fragments
of IgG1 and IgG3 to be compatible with Fab and Fc, whereas IgG2 and IgG4 rendered Fab2 …
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