Angiotensin I-converting enzyme in isolated human glomeruli

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Abstract

Angiotensin I-converting enzyme (ACE) activity was measured with hippurylhistidylleucine as a substrate in isolated human glomeruli. The mean level was 2.2±0.47 mIU/mg glomerular protein. S9780, a newly designed competitive inhibitor of ACE, inhibited this activity by 85% at 0.3 μM. [3H]S9780 specifically bound to isolated human glomeruli. The Kd value and the number of sites were 23 nM and 83 fmol/mg, respectively. The prodrug, S9490, and Captopril were less potent than S9780 in displacing [3H]S9780 from its binding sites. Angiotensin I had no effect. Binding of [3H]S9780 was inhibited after preincubation of the glomeruli with a specific polyclonal anti-human ACE antibody. These results demonstrate that ACE is present in human adult glomeruli. © 1987.

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Chansel, D., Morin, J. P., Borghi, H., Ardaillou, N., & Ardaillou, R. (1987). Angiotensin I-converting enzyme in isolated human glomeruli. FEBS Letters, 220(1), 247–252. https://doi.org/10.1016/0014-5793(87)80914-6

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