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- W3149485875 abstract "The mechanism of action of peptide inhibitors on angiotensin I-converting enzyme (Al-converting enzyme) was studied in relation to the substrate requirements of the enzyme in vivo in the dog lung and in vitro in plasma. 1- d -Asp-8-Ile-AI prepared by the solid-phase technique was compared with the known peptide inhibitors of Al-converting enzyme. BPP 5a (Pyr-Lys-Trp-Ala-Pro) and SQ 20881 (Pyr-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro) 125 I-1- d -Asp-8-Ile-AI was evaluated for susceptibility to cleavage by the Al-converting enzyme. In vitro and in vivo, 125 I-1- d -Asp-8-Ile-AI or BPP 5a in 50,000-fold molar excess produced only a slight delay in conversion of 125 1-AI to 125 I-angiotension II (AII); SQ 20881 blocked conversion completely. In vivo, l- d -Asp-8-Ile-AI or BPP 5a injected into the pulmonary circulation in 250-fold molar excess (250 nmole/kg) did not cause a diminution in the pressor response to AI administered 30 seconds later; SQ 20881 blocked the pressor response to Al for 60-90 minutes. 1- d -Asp-8-Ile-AI was a poor substrate for converting enzyme, since 125 I-1- d -Asp-8-Ile-AI was not converted to 125 I-1- d -Asp-8-Ile-AII, and unlabeled 1- d -Asp-8-Ile-AI did not block the pressor response to exogenous AII. 125 I-1- d -Asp-8-lle-AI was stable in plasma and in the pulmonary circulation The results suggest that since 1- d -Asp-8-Ile-AI is neither a substrate nor a blocker, substitution of the aliphatic residue Ile in the 8 position of AI may prevent binding to an active site in the AI-converting enzyme." @default.
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- W3149485875 date "1974-01-01" @default.
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- W3149485875 title "Structural Requirements for Substrates and Inhibitors of Angiotensin I-Converting Enzyme In Vivo and In Vitro" @default.
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- W3149485875 doi "https://doi.org/10.1161/01.res.34.1.19" @default.
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