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Angiotensin-converting activity of tissue kallikrein
M Ideishi1, M Sasaguri, M Ikeda
1Department of Internal Medicine, Fukuoka University School of Medicine, Japan.
Abstract:
This study examined the ability of tissue kallikreins, purified from both rat submandibular gland (SMG) and human urine, to form angiotensin II from synthetic angiotensin I. Both kallikreins converted angiotensin I to angiotensin II at neutral pH with the following kinetic constants: SMG kallikrein, Km = 9.43 x 10(-5) mol/l, Kcat = 1.58 mumols/mg protein/min; human urinary kallikrein, Km = 1.71 x 10(-4) mol/l, Kcat = 0.06 mumol/mg protein/min. These activities were not affected by angiotensin-converting enzyme (ACE) inhibitor. These results suggest that tissue kallikrein might participate in the formation of angiotensin II during administration of an ACE inhibitor.
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