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.
MeSH terms
- Amino Acid Sequence
- Angiotensin-Converting Enzyme Inhibitors / chemistry
- Angiotensin-Converting Enzyme Inhibitors / isolation & purification*
- Angiotensin-Converting Enzyme Inhibitors / pharmacology*
- Animals
- Antihypertensive Agents / chemistry
- Antihypertensive Agents / isolation & purification
- Antihypertensive Agents / pharmacology
- Chromatography, Gel
- Chromatography, High Pressure Liquid / methods
- Chromatography, Ion Exchange / methods
- Gliadin / chemistry*
- Inhibitory Concentration 50
- Male
- Peptidyl-Dipeptidase A / metabolism
- Protein Hydrolysates / chemistry*
- Rats
- Rats, Inbred SHR
- Triticum / chemistry
Substances
- Angiotensin-Converting Enzyme Inhibitors
- Antihypertensive Agents
- Protein Hydrolysates
- Gliadin
- Peptidyl-Dipeptidase A