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In this investigation, the ACE inhibitory phosphopeptides of T-1 was further purified by ultrafiltration and Sephadex G-15 column chromatography. ACE inhibitory activity was fractionated into three major phosphopeptides fractions of T-1-1,T-1-2 and T-1-3 in the pepsin hydrolyzates of the T-1 by gel filtration rechromatography on Sephadex G-15. The inhibition of ACE of the three kinds of phosphopeptides fractions (T-1-1,T-1-2 and T-1-3) was analyzed in vitro. The IC_\u003c50\u003e values of T-1-1,T-1-2 and T-1-3 of phosphopeptides for ACE were 0.159,0.095 and 0.140 mg protein/ml, respectively. The T-1-2 fraction had the most potent inyhibitory activity and showed 0.095 mg protein/ml inhibition against ACE at IC_\u003c50\u003e value. It has been demonstrated that the T-1-1,T-1-2 and T-1-3 contained about 33.3%, 3.01% and 27.12% as phosphonate-phosphorus of total phosphorus. The amino acid compositions of the phosphopeptides fractions (T-1-1,T-1-2 and T-1-3) were characterized by relatively high percentage for Tyr, Ser, Arg, Ala, Asp and Phe. When the ACE inhibitory phosphopeptides were analyzed by thin layer chromatography, some ninhydrine-positive spots were observed. 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Inhibitory Activity of Angiotensin 1-Converting Enzyme of Phosphopeptides Obtained from Proteolytic Hydrolyzates of Oyster, Crassostrea gigas
http://hdl.handle.net/10069/6087
http://hdl.handle.net/10069/6087e2ece402-b844-4e4a-ace3-719693099736
名前 / ファイル | ライセンス | アクション |
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Item type | 紀要論文 / Departmental Bulletin Paper(1) | |||||
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公開日 | 2007-02-08 | |||||
タイトル | ||||||
タイトル | Inhibitory Activity of Angiotensin 1-Converting Enzyme of Phosphopeptides Obtained from Proteolytic Hydrolyzates of Oyster, Crassostrea gigas | |||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | departmental bulletin paper | |||||
著者 |
Tamari, Masato
× Tamari, Masato× Kai, Masae× Kanda, Hiroko |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | In the previous papers^(1.2), we investigated the effects of ACE inhibitory activities of phosphopeptides of P-1 and C-2 which were obtained from edible oyster by proteolytic hydrolyzation. In this investigation, the ACE inhibitory phosphopeptides of T-1 was further purified by ultrafiltration and Sephadex G-15 column chromatography. ACE inhibitory activity was fractionated into three major phosphopeptides fractions of T-1-1,T-1-2 and T-1-3 in the pepsin hydrolyzates of the T-1 by gel filtration rechromatography on Sephadex G-15. The inhibition of ACE of the three kinds of phosphopeptides fractions (T-1-1,T-1-2 and T-1-3) was analyzed in vitro. The IC_<50> values of T-1-1,T-1-2 and T-1-3 of phosphopeptides for ACE were 0.159,0.095 and 0.140 mg protein/ml, respectively. The T-1-2 fraction had the most potent inyhibitory activity and showed 0.095 mg protein/ml inhibition against ACE at IC_<50> value. It has been demonstrated that the T-1-1,T-1-2 and T-1-3 contained about 33.3%, 3.01% and 27.12% as phosphonate-phosphorus of total phosphorus. The amino acid compositions of the phosphopeptides fractions (T-1-1,T-1-2 and T-1-3) were characterized by relatively high percentage for Tyr, Ser, Arg, Ala, Asp and Phe. When the ACE inhibitory phosphopeptides were analyzed by thin layer chromatography, some ninhydrine-positive spots were observed. These results suggest that the phosphopeptides are a mixture of several phosphopeptides. | |||||
書誌情報 |
長崎大学教育学部紀要. 自然科学 巻 63, p. 39-48, 発行日 2000-06 |
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ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 13451359 | |||||
書誌レコードID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AA11330079 | |||||
sortkey | ||||||
P00039-P00048 | ||||||
引用 | ||||||
内容記述タイプ | Other | |||||
内容記述 | 長崎大学教育学部紀要. 教育科学. vol.67, p.21-28; 2004@@@長崎大学教育学部紀要. 自然科学. vol.63, p.39-48; 2000 |