{"created":"2023-06-19T09:50:32.597378+00:00","id":7431,"links":{},"metadata":{"_buckets":{"deposit":"69dcc64c-ac9d-40e3-bafd-df1c3401d57c"},"_deposit":{"created_by":3,"id":"7431","owners":[3],"pid":{"revision_id":0,"type":"depid","value":"7431"},"status":"published"},"_oai":{"id":"oai:fukuyama-u.repo.nii.ac.jp:00007431","sets":["502:506:653:657"]},"author_link":["40866","40863","40870","40867","40869","40864","40862","40865","40868"],"item_1_biblio_info_14":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"1993-12","bibliographicIssueDateType":"Issued"},"bibliographicPageEnd":"12","bibliographicPageStart":"1","bibliographicVolumeNumber":"4","bibliographic_titles":[{"bibliographic_title":"福山大学附属内海生物資源研究所報告"}]}]},"item_1_creator_6":{"attribute_name":"著者名(日)","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"吉田, 美夫"}],"nameIdentifiers":[{"nameIdentifier":"40862","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"沖増, 英治"}],"nameIdentifiers":[{"nameIdentifier":"40863","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"雨村, 明倫"}],"nameIdentifiers":[{"nameIdentifier":"40864","nameIdentifierScheme":"WEKO"}]}]},"item_1_description_1":{"attribute_name":"ページ属性","attribute_value_mlt":[{"subitem_description":"P(論文)","subitem_description_type":"Other"}]},"item_1_description_11":{"attribute_name":"抄録(日)","attribute_value_mlt":[{"subitem_description":"ニジマス白血球の15-LO酵素の分子量は約70,000であり,哺乳類の15-LO酵素の分子量とも類似していた。至適反応pHは7.5であり,これも至適反応pH7.0をもつ哺乳類と類似していた。しかし,至適反応温度は15℃であり,これは至適反応温度を高温領域にもつ哺乳類とは異なっていた。ニジマス白血球の15-LO酵素の最終精製段階における回収率は3.1%,精製純度が4.8倍と非常に不安定な酵素であることが明らかになった。","subitem_description_type":"Other"}]},"item_1_description_12":{"attribute_name":"抄録(英)","attribute_value_mlt":[{"subitem_description":"15-Lipoxygenase activity with arachidonic acid as a substrate was detected in leukocyte extract from the kidney of rainbow trout (Oncorhynchus mykiss). 15-Lipoxygenase was purified by gel filtration followed by hydroxyapatite chromatography. The enzyme activity towards arachdonic acid was highest at pH 7.5 and at temperatures between 10℃ and 20℃. The molecular weight of enzyme estimated by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS-PAGE) was 70,000 near that of the enzyme from human leukocyte (65,000-75,000)[E.Sigal et.al : J. Biol. Chem., 263, 5328-5332(1988)].","subitem_description_type":"Other"}]},"item_1_full_name_7":{"attribute_name":"著者名よみ","attribute_value_mlt":[{"nameIdentifiers":[{"nameIdentifier":"40865","nameIdentifierScheme":"WEKO"}],"names":[{"name":"ヨシダ, ヨシオ"}]},{"nameIdentifiers":[{"nameIdentifier":"40866","nameIdentifierScheme":"WEKO"}],"names":[{"name":"オキマス, エイジ"}]},{"nameIdentifiers":[{"nameIdentifier":"40867","nameIdentifierScheme":"WEKO"}],"names":[{"name":"アメムラ, アキノリ"}]}]},"item_1_full_name_8":{"attribute_name":"著者名(英)","attribute_value_mlt":[{"nameIdentifiers":[{"nameIdentifier":"40868","nameIdentifierScheme":"WEKO"}],"names":[{"name":"Yoshida, Yoshio","nameLang":"en"}]},{"nameIdentifiers":[{"nameIdentifier":"40869","nameIdentifierScheme":"WEKO"}],"names":[{"name":"Okimasu, Eiji","nameLang":"en"}]},{"nameIdentifiers":[{"nameIdentifier":"40870","nameIdentifierScheme":"WEKO"}],"names":[{"name":"Amemura, Akinori","nameLang":"en"}]}]},"item_1_source_id_13":{"attribute_name":"雑誌書誌ID","attribute_value_mlt":[{"subitem_source_identifier":"AN10409073","subitem_source_identifier_type":"NCID"}]},"item_1_text_10":{"attribute_name":"著者所属(英)","attribute_value_mlt":[{"subitem_text_language":"en","subitem_text_value":"Research Institute of Marine Bioresources, Fukuyama University"},{"subitem_text_language":"en","subitem_text_value":"Research Institute of Marine Bioresources, Fukuyama University"},{"subitem_text_language":"en","subitem_text_value":"Research Institute of Marine Bioresources, Fukuyama University"}]},"item_1_text_2":{"attribute_name":"記事種別(日)","attribute_value_mlt":[{"subitem_text_value":"報文"}]},"item_1_text_3":{"attribute_name":"記事種別(英)","attribute_value_mlt":[{"subitem_text_language":"en","subitem_text_value":"Original Paper"}]},"item_1_text_9":{"attribute_name":"著者所属(日)","attribute_value_mlt":[{"subitem_text_value":"福山大学内海生物資源研究所:(現)共立商事(株)中央研究所"},{"subitem_text_value":"福山大学内海生物資源研究所"},{"subitem_text_value":"福山大学内海生物資源研究所"}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"1993-12-01"}],"displaytype":"detail","filename":"KJ00005783761.pdf","filesize":[{"value":"1.0 MB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"url":"https://fukuyama-u.repo.nii.ac.jp/record/7431/files/KJ00005783761.pdf"},"version_id":"5a5c0f90-57be-4f2a-8695-66a895fef0fd"}]},"item_language":{"attribute_name":"言語","attribute_value_mlt":[{"subitem_language":"jpn"}]},"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":"ニジマス白血球のアラキドン酸15-リポキシゲナーゼの精製とその諸性質","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"ニジマス白血球のアラキドン酸15-リポキシゲナーゼの精製とその諸性質"},{"subitem_title":"Purification and Characterization of Arachidonate 15-Lipoxygenase from Leukocytes of Rainbow Trout(Oncorhynchus mykiss)","subitem_title_language":"en"}]},"item_type_id":"1","owner":"3","path":["657"],"pubdate":{"attribute_name":"公開日","attribute_value":"1993-12-01"},"publish_date":"1993-12-01","publish_status":"0","recid":"7431","relation_version_is_last":true,"title":["ニジマス白血球のアラキドン酸15-リポキシゲナーゼの精製とその諸性質"],"weko_creator_id":"3","weko_shared_id":-1},"updated":"2023-06-19T10:43:13.488322+00:00"}