STRUCTURES AND ACTIVITY OF ANGIOTENSIN-CONVERTING ENZYME-INHIBITORS IN AN ALPHA-ZEIN HYDROLYSATE

被引：217

作者：

MIYOSHI, S ^{[1
]}

ISHIKAWA, H ^{[1
]}

KANEKO, T ^{[1
]}

FUKUI, F ^{[1
]}

TANAKA, H ^{[1
]}

MARUYAMA, S ^{[1
]}

机构：

[1] FERMENTAT RES INST,TSUKUBA,IBARAKI 305,JAPAN

来源：

AGRICULTURAL AND BIOLOGICAL CHEMISTRY | 1991年 / 55卷 / 05期

关键词：

D O I：

10.1080/00021369.1991.10870760

中图分类号：

S3 [农学（农艺学）];

学科分类号：

0901 ;

摘要：

Peptides that inhibit angiotensin-converting enzyme (ACE) were isolated from alpha-zein hydrolysate prepared with thermolysin. Their chemical structures were identified by Edman degradation and fast-atom bombardment mass spectrometry. Most of them were found to be tripeptides such as Leu-Arg-Pro, Leu-Ser-Pro, and Leu-Gln-Pro, having IC50 values of 0.27, 1.7, and 1.9-mu-M, respectively. These peptides were synthesized by a solid phase procedure and had similar ACE inhibitory activities as the isolated inhibitors. The hypotensive activity of Leu-Arg-Pro on spontaneously hypertensive rats was also investigated, with the result that the blood pressure decreased by 15 mmHg after a 30 mg/kg intravenous injection.

引用

页码：1313 / 1318

页数：6

共 21 条

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