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Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides from wheat gliadin hydrolysate

✍ Scribed by Motoi, Hirofumi ;Kodama, Toshiaki

Publisher
John Wiley and Sons
Year
2003
Tongue
English
Weight
589 KB
Volume
47
Category
Article
ISSN
0027-769X

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✦ Synopsis

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 (IC~50~ value) was 2.7 μM. 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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