An arginine carboxypeptidase (CPR) is generated from its precursor (ProCPR) by proteolytic enzyme and may function in vivo in the removal of C-terminal arginine from inflammatory peptides such as C3a and C5a. We studied changes in this enzyme activity in rats submitted to liver cirrhois, hepatectomy, splenectomy, burning or endotoxin challenge. It is suggested that this enzyme could be activated with simultaneous generation of active peptides such as C3a and C5a at inflammatory sites to prevent their excess activity and inactivated due to its instability.
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Kato et al. (1994) studied this question.
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