PURIFICATION AND IDENTIFICATION OF AN ANGIOTENSIN I-CONVERTING ENZYME-INHIBITOR FROM SOY-SAUCE

被引：164

作者：

KINOSHITA, E

YAMAKOSHI, J

KIKUCHI, M

机构：

[1] Research and Development Division, Kikkoman Corporation, 399 Noda, Noda-shi

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1993年 / 57卷 / 07期

关键词：

D O I：

10.1271/bbb.57.1107

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The inhibitory activity of an angiotensin I-converting enzyme (ACE) detected in soy sauce was fractionated into two major fractions of high molecular weight (Hw) and low molecular weight (Lw) by gel filtration chromatography on Bio-gel P-2 after treating with ethanol. The Hw fraction reduced the blood pressure in hypertensive rats after orally administering, while the Lw fraction did not. The ACE inhibitor in the Hw fraction was further purified by Dowex 50W ion-exchange chromatography and four subsequent steps of HPLC. On the basis of the SIMS-mass spectrum, NMR spectrum and other characteristics, the purified ACE inhibitor was identified as nicotianamine (N-[N-(3-amino-3-carboxypropyl)-3-amino-3-carboxypropyl]azetidine-2-carboxylic acid). The IC50 value for this ACE was 0.26 muM.

引用

页码：1107 / 1110

页数：4

共 26 条

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