title: Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle.
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.
authors.affiliation: Department of Food Science and Technology, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Matsufuji
authors.forename: T
authors.initials: T
authors.lastname: Matsui
authors.forename: E
authors.initials: E
authors.lastname: Seki
authors.forename: K
authors.initials: K
authors.lastname: Osajima
authors.forename: M
authors.initials: M
authors.lastname: Nakashima
authors.forename: Y
authors.initials: Y
authors.lastname: Osajima
mesh_terms: D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000302:isolation & purification* / Q000494:pharmacology; D000818:Animals; D010450:Endopeptidases / Q000737:chemistry*; D005399:Fishes; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008969:Molecular Sequence Data; D009132:Muscles / Q000201:enzymology; D010455:Peptides / Q000302:isolation & purification* / Q000494:pharmacology; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D010455:Peptides; D010450:Endopeptidases; D007703:Peptidyl-Dipeptidase A