Journal
NAHRUNG-FOOD
Volume 47, Issue 5, Pages 354-358Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/food.200390081
Keywords
angiotensin-converting enzyme inhibitor; bioactive peptide; functional food; hypertension; wheat gliadin hydrolysate
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Angiotensin I-converting enzyme (ACE) inhibitory peptide was isolated from wheat gliadin hydrolysate prepared with acid protease. Consecutive purification methods were used for peptide isolation including ion-exchange chromatography, size-exclusion chromatography, and reverse-phase high-performance liquid chromatography. The amino acid sequence of this peptide was identified as Ile-Ala-Pro, and the ACE inhibitory activity (IC50 value) was 2.7 muM. The hypotensive activity of Ile-Ala-Pro on spontaneously hypertensive rats was investigated. This peptide inhibited the hypertensive activity of angiotensin I with intravenous injection, and decreased the blood pressure significantly with intraperitoneal administration.
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