Abstract
Oligopeptides which inhibit angiotensin I converting enzyme (ACE) were studied by industrial methods and isolated from the hydrolyzate of sardine muscle with Denazyme AP. The preparation involved QAE-Sephadex A-25, SP-Sephadex C-25 and Bio-Gel P-2 followed by high performance liquid chromatography. Five dipeptides were identified. The amino acid sequences of these dipeptides analyzed by the Edman procedure were Tyr-Pro, Val-Phe, Ile-Phe, Trp-Ile and Trp-Leu. The IC50 values of these dipeptides for ACE from rabbit lung were 2440, 250, 100, 82, and 51μM, respectively. The corresponding synthetic peptides were found to be identical with the isolated inhibitors in the ACE inhibitory activities.
