Purification and Identification of an Angiotensin I-converting Enzyme Inhibitor from Soy Sauce
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概要
- 論文の詳細を見る
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 IC_<50> value for this ACE was 0.26μM.
- 社団法人日本農芸化学会の論文
- 1993-07-23
著者
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YAMAKOSHI Jun
Research and Development Division, Kikkoman Corporation
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KIKUCHI Mamoru
Research and Development Division, Kikkoman Corporation
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Yamakoshi Jun
Research And Development Division Kikkoman Corporation
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Kikuchi Mamoru
Research And Development Division Kikkoman Corporation
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Kikuchi Mamoru
Research & Development Division Kikkoman Corporation
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Kinoshita Emiko
Research and Development Division, Kikkoman Corporation
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Yamakoshi J
Research And Development Division Kikkoman Corporation
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Kinoshita E
Kikkoman Corp. Chiba Jpn
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Kinoshita Emiko
Research & Development Division Kikkoman Corporation
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