title: Pro-carboxypeptidase R cleaves bradykinin following activation.
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.
authors.affiliation: First Department of Surgery, Fukuoka University School of Medicine, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Shinohara
authors.forename: C
authors.initials: C
authors.lastname: Sakurada
authors.forename: T
authors.initials: T
authors.lastname: Suzuki
authors.forename: O
authors.initials: O
authors.lastname: Takeuchi
authors.forename: W
authors.initials: W
authors.lastname: Campbell
authors.forename: S
authors.initials: S
authors.lastname: Ikeda
authors.forename: N
authors.initials: N
authors.lastname: Okada
authors.forename: H
authors.initials: H
authors.lastname: Okada
mesh_terms: D001920:Bradykinin / Q000378:metabolism*; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000378:metabolism; D006801:Humans; D001121:Lysine Carboxypeptidase / Q000378:metabolism*; D008297:Male; D011498:Protein Precursors / Q000378:metabolism
chemical_list: D004792:Enzyme Precursors; D011498:Protein Precursors; D001121:Lysine Carboxypeptidase; D001920:Bradykinin