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

Volume: 47, Issue: 5, Pages: 354 - 358
Published: Oct 1, 2003
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...
Paper Details
Title
Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides from wheat gliadin hydrolysate.
Published Date
Oct 1, 2003
Volume
47
Issue
5
Pages
354 - 358
Citation AnalysisPro
  • Scinapse’s Top 10 Citation Journals & Affiliations graph reveals the quality and authenticity of citations received by a paper.
  • Discover whether citations have been inflated due to self-citations, or if citations include institutional bias.