{"created":"2023-05-15T16:47:13.949993+00:00","id":23816,"links":{},"metadata":{"_buckets":{"deposit":"f86b98de-9ed2-4cb3-a10a-2e742ca9c952"},"_deposit":{"created_by":2,"id":"23816","owners":[2],"pid":{"revision_id":0,"type":"depid","value":"23816"},"status":"published"},"_oai":{"id":"oai:nagasaki-u.repo.nii.ac.jp:00023816","sets":["18:105:117:1673"]},"author_link":["100492","100496","100493","100491","100495","100494"],"item_3_alternative_title_19":{"attribute_name":"その他のタイトル","attribute_value_mlt":[{"subitem_alternative_title":"Inhibitory Activity of Angiotensin 1-Converting Enzyme of Phosphopeptides Obtained from Proteolytic Hydrolyzates of Oyster,Crassostrea gigas"}]},"item_3_biblio_info_6":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2000-03","bibliographicIssueDateType":"Issued"},"bibliographicPageEnd":"40","bibliographicPageStart":"29","bibliographicVolumeNumber":"62","bibliographic_titles":[{"bibliographic_title":"長崎大学教育学部紀要. 自然科学"}]}]},"item_3_description_4":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"In this investigation, the ACE inhibitory phosphopeptides of P-1 and C-2 were further purified by ultrafiltration and by Sephadex G-15 chromatography. ACE inhibitory activity was fractionated into three major phosphopeptides fractions of P-1-1,P-1-2 and P-1-3 in the pepsin hydrolyzates of the P-1,and into fractions of C-2-1,C-2-2 and C-2-3 in the pepsin hydrolyzates of the C-2 by gel filtration rechromatography on Sephadex G-15,respectively. The inhibition of ACE of the six kinds of phosphopeptides fractions (P-1-1,P-1-2,P-1-3,C-2-1,C-2-2 and C-2-3) was analyzed in vitro. The IC_<50> values of P-1-1,P-1-2,P-1-3,C-2-1,C-2-2 and C-2-3 of phosphopeptides for ACE were 1.11,0.04,0.05,1.04,0.72 and 0.06mg protein/ml, respectively. The P-1-2 fraction had the most inhibitory activity and showed 0.04mg protein/ml inhibition against ACE at IC_<50> value. It has been demonstrated that the P-1-1,P-1-2,P-1-3,C-2-1,C-2-2 and C-2-3 contained about 23.2%, 4.4%, 28.1%, 2.0%, 3.8% and 1.6% as phosphonate-phosphorus of total phosphorus. The amino acid compositions of the phosphopeptides fractions (P-1-1,P-1-2,P-1-3,C-2-1,C-2-2 and C-2-3) were characterized by relatively high percentage for Glu, Asp, Gly, Ala, Val, Leu, Tyr, Phe, Lys and Arg. 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. The results above, the Sephadex G-15 gel filtration patterns of the active fraction obtained from the Sephadex G-50 column chromatography indicated that the molecular weight of the phosphopeptide was about 200 &acd; 1000.","subitem_description_type":"Abstract"}]},"item_3_description_64":{"attribute_name":"引用","attribute_value_mlt":[{"subitem_description":"長崎大学教育学部紀要. 教育科学. vol.66, p.25-39; 2004@@@長崎大学教育学部紀要. 自然科学. vol.62, p.29-40; 2000","subitem_description_type":"Other"}]},"item_3_full_name_3":{"attribute_name":"著者別名","attribute_value_mlt":[{"nameIdentifiers":[{"nameIdentifier":"100495","nameIdentifierScheme":"WEKO"}],"names":[{"name":"Tamari, Masato"}]},{"nameIdentifiers":[{"nameIdentifier":"100496","nameIdentifierScheme":"WEKO"}],"names":[{"name":"Kanda, Hiroko"}]}]},"item_3_source_id_10":{"attribute_name":"書誌レコードID","attribute_value_mlt":[{"subitem_source_identifier":"AA11330079","subitem_source_identifier_type":"NCID"}]},"item_3_source_id_7":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"13451359","subitem_source_identifier_type":"ISSN"}]},"item_3_text_62":{"attribute_name":"sortkey","attribute_value_mlt":[{"subitem_text_value":"P00029-P00040"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"玉利, 正人"}],"nameIdentifiers":[{"nameIdentifier":"100491","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"神田, 浩子"}],"nameIdentifiers":[{"nameIdentifier":"100492","nameIdentifierScheme":"WEKO"}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2020-12-24"}],"displaytype":"detail","filename":"KJ00000045788.pdf","filesize":[{"value":"682.6 kB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"KJ00000045788.pdf","url":"https://nagasaki-u.repo.nii.ac.jp/record/23816/files/KJ00000045788.pdf"},"version_id":"cec17d5d-2444-4486-9540-61ed4edf9e53"}]},"item_language":{"attribute_name":"言語","attribute_value_mlt":[{"subitem_language":"eng"}]},"item_resource_type":{"attribute_name":"資源タイプ","attribute_value_mlt":[{"resourcetype":"departmental bulletin paper","resourceuri":"http://purl.org/coar/resource_type/c_6501"}]},"item_title":"食用カキのタンパク質分解酵素による分解物から得られたリンペプチドによるACEの阻害活性","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"食用カキのタンパク質分解酵素による分解物から得られたリンペプチドによるACEの阻害活性"}]},"item_type_id":"3","owner":"2","path":["1673"],"pubdate":{"attribute_name":"公開日","attribute_value":"2007-02-08"},"publish_date":"2007-02-08","publish_status":"0","recid":"23816","relation_version_is_last":true,"title":["食用カキのタンパク質分解酵素による分解物から得られたリンペプチドによるACEの阻害活性"],"weko_creator_id":"2","weko_shared_id":-1},"updated":"2023-05-16T00:36:21.305238+00:00"}