title: Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides from wheat gliadin hydrolysate.
abstract: 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 microM. 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.
authors: Research Center for Basic Science, Research and Development, Quality Assurance Division Nisshin Seifun Group Inc., Iruma-Gun, Saitama, Japan. motoih@mail.ni-net.co.jp
authors: Hirofumi
authors: H
authors: Motoi
authors: Toshiaki
authors: T
authors: Kodama
mesh_terms: D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology*; D000818:Animals; D000959:Antihypertensive Agents / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D002852:Chromatography, Ion Exchange / Q000379:methods; D005903:Gliadin / Q000737:chemistry*; D020128:Inhibitory Concentration 50; D008297:Male; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism; D011492:Protein Hydrolysates / Q000737:chemistry*; D051381:Rats; D011918:Rats, Inbred SHR; D014908:Triticum / Q000737:chemistry
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D000959:Antihypertensive Agents; D011492:Protein Hydrolysates; D005903:Gliadin; D007703:Peptidyl-Dipeptidase A