{"created":"2023-05-15T16:47:14.216126+00:00","id":23822,"links":{},"metadata":{"_buckets":{"deposit":"06d34a96-0ae4-485c-ae13-5e36f9b295e3"},"_deposit":{"created_by":2,"id":"23822","owners":[2],"pid":{"revision_id":0,"type":"depid","value":"23822"},"status":"published"},"_oai":{"id":"oai:nagasaki-u.repo.nii.ac.jp:00023822","sets":["18:105:117:1674"]},"author_link":["100522","100523","100521"],"item_3_biblio_info_6":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2000-06","bibliographicIssueDateType":"Issued"},"bibliographicPageEnd":"48","bibliographicPageStart":"39","bibliographicVolumeNumber":"63","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 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.","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.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","subitem_description_type":"Other"}]},"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":"P00039-P00048"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"Tamari, Masato"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Kai, Masae"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Kanda, Hiroko"}],"nameIdentifiers":[{}]}]},"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":"KJ00000045799.pdf","filesize":[{"value":"561.8 kB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"KJ00000045799.pdf","url":"https://nagasaki-u.repo.nii.ac.jp/record/23822/files/KJ00000045799.pdf"},"version_id":"e915e6c2-ffc2-4d7b-99a2-efa7eac2e962"}]},"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":"Inhibitory Activity of Angiotensin 1-Converting Enzyme of Phosphopeptides Obtained from Proteolytic Hydrolyzates of Oyster, Crassostrea gigas","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"Inhibitory Activity of Angiotensin 1-Converting Enzyme of Phosphopeptides Obtained from Proteolytic Hydrolyzates of Oyster, Crassostrea gigas"}]},"item_type_id":"3","owner":"2","path":["1674"],"pubdate":{"attribute_name":"公開日","attribute_value":"2007-02-08"},"publish_date":"2007-02-08","publish_status":"0","recid":"23822","relation_version_is_last":true,"title":["Inhibitory Activity of Angiotensin 1-Converting Enzyme of Phosphopeptides Obtained from Proteolytic Hydrolyzates of Oyster, Crassostrea gigas"],"weko_creator_id":"2","weko_shared_id":-1},"updated":"2023-05-16T00:36:13.714262+00:00"}