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Pro-carboxypeptidase R cleaves bradykinin following activation
T Shinohara1, C Sakurada, T Suzuki
1First Department of Surgery, Fukuoka University School of Medicine, Japan.
International Archives of Allergy and Immunology
|January 1, 1994
Abstract:
Arginine carboxypeptidase (CPR) is a labile enzyme present in human serum which is unrelated to carboxypeptidase N. In this study we demonstrate that CPR exists in a precursor form in plasma and can be converted to the active form by trypsin and presumable trypsin-like enzymes. The trypsin-generated active form can not only cleave a small synthetic substrate, hippuryl-L-arginine, but can remove terminal arginine from bradykinin.