从小麦醇溶蛋白水解物中分离及鉴定血管紧张素I转换酶抑制肽

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

作者信息

Motoi Hirofumi, Kodama Toshiaki

机构信息

Research Center for Basic Science, Research and Development, Quality Assurance Division Nisshin Seifun Group Inc., Iruma-Gun, Saitama, Japan.

出版信息

Nahrung. 2003 Oct;47(5):354-8. doi: 10.1002/food.200390081.

DOI:10.1002/food.200390081

PMID:14609094

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.

摘要

从用酸性蛋白酶制备的小麦醇溶蛋白水解物中分离出血管紧张素I转换酶（ACE）抑制肽。采用连续纯化方法分离该肽，包括离子交换色谱法、尺寸排阻色谱法和反相高效液相色谱法。该肽的氨基酸序列被鉴定为Ile-Ala-Pro，其ACE抑制活性（IC50值）为2.7微摩尔。研究了Ile-Ala-Pro对自发性高血压大鼠的降压活性。该肽静脉注射可抑制血管紧张素I的升压活性，腹腔给药可显著降低血压。