Structures and activity of angiotensin-converting enzyme inhibitors in an α-zein hydrolysate
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- MIYOSHI Shinsuke
- Research and Development Center, Showa Sangyo Co., Ltd.
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- ISHIKAWA Hiromi
- Research and Development Center, Showa Sangyo Co., Ltd.
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- KANEKO Toshiyuki
- Research and Development Center, Showa Sangyo Co., Ltd.
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- FUKUI Fumio
- Research and Development Center, Showa Sangyo Co., Ltd.
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- TANAKA Hideoki
- Fermentation Research Institute
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- MARUYAMA Susumu
- Fermentation Research Institute
書誌事項
- タイトル別名
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- Structures and activity of angiotensin-converting enzyme inhibitors in an .ALPHA.-zein hydrolysate.
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抄録
Peptides that inhibit angiotensin-converting enzyme (ACE) were isolated from α-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-Gin-Pro, having IC50 values of 0.27, 1.7, and 1.9μM, 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 15mmHg after a 30mg/kg intravenous injection.
収録刊行物
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- Agricultural and Biological Chemistry
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Agricultural and Biological Chemistry 55 (5), 1313-1318, 1991
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390282681439483136
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- NII論文ID
- 110006325540
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- NII書誌ID
- AA00515312
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- COI
- 1:CAS:528:DyaK3MXmsVOntro%3D
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- ISSN
- 18811280
- 00021369
- http://id.crossref.org/issn/00021369
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- PubMed
- 1368684
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- Crossref
- PubMed
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可