Three peptides (I:Leu-Lys-Leu, II:Val-Lys-Ala-Gly-Phe, and III: Lys-Val-Leu-Ala-Gly-Met) from a hydrolyzate of sardine muscle and that inhibited angiotensin I converting enzyme were digested with the intestinal fluid of pigs. The IC
50 values of II and III were decreased to 56% and 66% of the original value, respectively, after digestion. Peptide I was not digested. Five peptide fragments were isolated from the peptide digests by high-pressure liquid chromatography. By the Edman procedure, peptide II digest was found to contain the fragments Val-Lys-Ala-Gly and Gly-Phe, and peptide III digest was found to contain the fragments Ala-Gly-Met, Lys-Val-Leu-Ala-Gly, and Lys-Val-Leu.
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