2016年11月
Galloylated Catechins as Potent Inhibitors of Angiotensin Converting Enzyme
FOOD SCIENCE AND TECHNOLOGY RESEARCH
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- 巻
- 22
- 号
- 6
- 開始ページ
- 847
- 終了ページ
- 851
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.3136/fstr.22.847
- 出版者・発行元
- KARGER
In the present study, we investigated the inhibitory effects of four tea catechins, including (-)-epicatechin (EC), (-)-epigallocatechin (EGC), (-)-epicatechin gallate (ECg) and (-)-epigallocatechin gallate (EGCg), on angiotensin converting enzyme (ACE) activity in vitro. Each catechin treatment significantly reduced the ACE activity with the order of potency being EGCg > ECg > EGC = EC. The addition of 1 mM borate significantly recovered the reduced ACE activities by tea catechins, suggesting that hydroxyl groups at the B-ring or at a galloyl moiety play an important role in the ACE-inhibitory mechanism. The covalent modification of ACE by tea catechins was also observed by a redox-cycling staining experiment. A Lineweaver-Burk plot indicated that EGC and ECg were noncompetitive inhibitors. The galloylated catechins might more potently inhibit ACE activity in an allosteric manner through the interaction of the galloyl moiety with the non-catalytic site of ACE.
- リンク情報
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- DOI
- https://doi.org/10.3136/fstr.22.847
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000389116500016&DestApp=WOS_CPL
- URL
- https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85007493456&origin=inward
- ID情報
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- DOI : 10.3136/fstr.22.847
- ISSN : 1344-6606
- SCOPUS ID : 85007493456
- Web of Science ID : WOS:000389116500016