Structures and activity of angiotensin-converting enzyme inhibitors in an α-zein hydrolysate

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タイトル別名
  • Structures and activity of angiotensin-converting enzyme inhibitors in an .ALPHA.-zein hydrolysate.

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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.

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詳細情報 詳細情報について

  • CRID
    1390282681439483136
  • NII論文ID
    110006325540
  • NII書誌ID
    AA00515312
  • DOI
    10.1271/bbb1961.55.1313
  • COI
    1:CAS:528:DyaK3MXmsVOntro%3D
  • ISSN
    18811280
    00021369
    http://id.crossref.org/issn/00021369
  • PubMed
    1368684
  • 本文言語コード
    en
  • データソース種別
    • JaLC
    • Crossref
    • PubMed
    • CiNii Articles
  • 抄録ライセンスフラグ
    使用不可

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