書誌事項
- タイトル別名
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- Peptides from Peptic Hydrolyzate of Heated Sardine Meat That Inhibit Angiotensin I Converting Enzyme.
- カネツ イワシ キンニク ノ ペプシン カスイ ブンカイブツチュウ ニ ソンザ
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説明
Three peptides that inhibited angiotensin I converting enzyme (ACE) were isolated from a peptic hydrolyzate of heated sardine muscle. The preparation involved SP-Sephadex C-25 and Toyopearl HW-40 chromatography followed by three steps of high-performance liquid chromatography. The amino acid sequences of these peptides, identified by Edman degradation, were: B-1, Val-Lys-Ala-Gly-Phe; B-2, Lys-Val-Leu-Ala-Gly-Met; and B-3, Leu-Lys-Leu. The IC50 values of these peptides for ACE from rabbit lung were 83, 30, and 188 μM, respectively. These peptides were synthesized by the solid-phase method, and the IC50 values of the synthetic peptides were similar to those of B-1, B-2, and B-3. These results indicated that all amino acids in B-1, B-2, and B-3 may be in the L-configuration. Fourteen kinds of actins derived from humans, rabbits, rats, mice, soy beans, maize, and so on contained the B-1 sequence of five amino acids.
収録刊行物
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- 日本農芸化学会誌
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日本農芸化学会誌 66 (1), 25-29, 1992
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
- 1390001204507214976
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- NII論文ID
- 130001228007
- 10011626895
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- NII書誌ID
- AN00196191
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- COI
- 1:CAS:528:DyaK38XitlCit7c%3D
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- ISSN
- 18836844
- 00021407
- http://id.crossref.org/issn/00021407
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- NDL書誌ID
- 3759462
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可
