Abstract
Three inhibitory peptides of angiotension I-converting enzyme (ACE) were isolated from fresh latex of the fig tree (Ficus carica). The amino acid sequences of these peptides identified by the Ed man procedure and carboxypeptidase digestion were: Ala-Val-Asn-Pro-Ile-Arg, Leu-Tyr-Pro-Val-Lys, and Leu-Val-Arg. The IC50 values of these peptides for ACE from rabbit lung were 13μM, 4.5μM, and 14μM, respectively. These peptides have been synthesized by the solid phase procedure, and the synthetic peptides were found to be identical with the natural inhibitors in their ACE inhibitory activities.
