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  • Title: Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle.
    Author: Matsufuji H, Matsui T, Seki E, Osajima K, Nakashima M, Osajima Y.
    Journal: Biosci Biotechnol Biochem; 1994 Dec; 58(12):2244-5. PubMed ID: 7765718.
    Abstract:
    The ACE inhibitory activity of an alkaline protease hydrolyzate from sardine muscle did not change after being treated by gastrointestinal proteases (IC50 = 0.082 mg protein/ml). Eleven new ACE inhibitory peptides, constructed with 2 to 4 amino acid residues, were isolated from the hydrolyzate. The ACE inhibitory activity of each was mostly below 100 microM of IC50 value; the maximal inhibitory activity was observed for Lys-Trp (IC50 = 1.63 microM). The isolated peptides inhibited ACE competitively, except for Met-Tyr with non-competitive inhibition. As the result of sequence homology, Arg-Val-Tyr isolated from the hydrolyzate was found in the primary structure of angiotensins I, II, and III, and of des As[1]-angiotensin I.
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