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Identification of an antihypertensive peptide derived from chicken bone extract
Author(s) -
NAKADE Koji,
KAMISHIMA Ryosuke,
INOUE Yusuke,
AHHMED Abdulatef,
KAWAHARA Satoshi,
NAKAYAMA Tatsuo,
MARUYAMA Masugi,
NUMATA Masahiro,
OHTA Kazuyoshi,
AOKI Takayoshi,
MUGURUMA Michio
Publication year - 2008
Publication title -
animal science journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.606
H-Index - 38
eISSN - 1740-0929
pISSN - 1344-3941
DOI - 10.1111/j.1740-0929.2008.00584.x
Subject(s) - peptide , angiotensin converting enzyme , chemistry , enzyme , renin–angiotensin system , blood pressure , pharmacology , digestion (alchemy) , biochemistry , amino acid , oral administration , peptide sequence , endocrinology , medicine , chromatography , gene
A novel angiotensin‐converting enzyme (ACE) inhibitory peptide was isolated and purified from chicken bone extract by enzymatic digestion. The peptide was defined as an ACE inhibitor, and it demonstrated antihypertensive activity following oral administration to spontaneously hypertensive rats (SHRs). The results of this study suggest that peptides derived from an extract of chicken bones, administered orally, have the ability to reduce the blood pressure of SHRs significantly over a short period of time (3 h). Moreover, the blood pressure then remains low for 3 h. This peptide derived from chicken bones may therefore have great value as a short‐term remedy for chronic conditions such as high blood pressure. The amino acid sequence of the peptide was YYRA (Tyr‐Tyr‐Arg‐Ala), which was the origin of the Ig heavy chain V region (27–30 position). The IC 50 value of its synthetic peptide was 33.9 μg/mL. We suggest that the ACE inhibitory and antihypertensive peptides derived from chicken bone extract may contribute to develop physiologically functional foods or improve food functionality.