Angiotensins are peptide hormone components of the renin-angiotensin system involved in the regulation of blood vessel constriction and aldosterone release. Angiotensin I, a decapeptide derived from angiotensinogen, is a converted to Angiotensin II by the removal of the two C-terminal amino acids. Various analogues of Angiotensin I may be used as substrates to identify, differentiate and characterize angiotensin-converting enzyme(s) (ACE).
The American journal of physiology, 273(6 Pt 2), R2089-R2096 (1998-01-22)
Our aim was to study the role of angiotensin-converting enzyme (ACE) and angiotensin II (ANG II) on ovarian steroidogenesis and prostaglandin production of amphibian. Hormonal effects of ACE, ACE inhibitors, synthetic bullfrog angiotensin I (ANG I), and [Val5]ANG II were
Journal of pharmacobio-dynamics, 9(7), 585-592 (1986-07-01)
In the present investigation, the occurrence of angiotensin I converting enzyme (EC 3.4.15.1; ACE) was first demonstrated in the kidney of bullfrog (Rana catesbeiana). Namely, a large amount of hydrolyzing activity toward N alpha-hippuryl-L-His-L-Leu-OH (HHL), a synthetic substrate of ACE
The occurrence of angiotensin converting enzyme (EC 3.4.15.1; ACE) was demonstrated for the first time in serum of newt (Triturus carnifex) and frog (Rana esculenta). The enzymatic activity was evidenced following hydrolysis of N-[3-(2-furyl) acryloyl]L-phenylalanyl glycyl glycine (FAPGG), a synthetic
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