{"created":"2023-05-15T13:38:59.684110+00:00","id":3068,"links":{},"metadata":{"_buckets":{"deposit":"0ac5fab0-bbe6-4bcc-b776-e018f0156664"},"_deposit":{"created_by":12,"id":"3068","owners":[12],"pid":{"revision_id":0,"type":"depid","value":"3068"},"status":"published"},"_oai":{"id":"oai:repository.naro.go.jp:00003068","sets":["87:627:628:388:402"]},"author_link":["1317"],"item_10002_biblio_info_7":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2015-03-01","bibliographicIssueDateType":"Issued"},"bibliographicPageEnd":"39","bibliographicPageStart":"35","bibliographicVolumeNumber":"79","bibliographic_titles":[{"bibliographic_title":"食品総合研究所研究報告"},{"bibliographic_title":"Report of National Food Research Institute","bibliographic_titleLang":"en"}]}]},"item_10002_description_5":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"The presence of a dehydrin-like protein in buckwheat seeds had been revealed using an antibody against a Lysrich conservative motif sequence for dehydrin. In this study, the dehydrin protein was purified from a Japanese variety of buckwheat seed (Fagopyrum esculentum cv. Kitawase) through four purification steps: heat treatment, addition of 10–45% saturated ammonium sulfate, ion-exchange chromatography on a HiTrap Q Fast Flow column, and gel filtration on a HiPrep Sephacryl S-200 column. Results of peptide mapping with trypsin indicated that the purified protein contained conservative motif sequences and Gly-rich sequences, which are characteristic to dehydrin proteins. The results of the pepsin digestion experiment showed that the purified dehydrin was promptly cleaved by simulated gastric fluid, and that a 16-kDa polypeptide that is highly resistant to pepsin digestion was produced.","subitem_description_type":"Abstract"}]},"item_10002_description_6":{"attribute_name":"内容記述","attribute_value_mlt":[{"subitem_description":"デハイドリンは、乾燥や低温によって誘導される植物ストレスタンパク質であり、種子にも広く分布することが知られている。前報において、デハイドリン固有のモチーフ配列に対する抗体を用いて、ソバ種子ならびに食品中にデハイドリン様タンパク質が存在することを示した。本研究では日本産ソバ種子（品種キタワセ）から、硫酸アンモニウム分画、イオン交換クロマトグラフィーおよびゲル濾過によって、20kDaデハイドリンを単離精製した。トリプシン消化物のアミノ酸配列分析の結果、デハイドリンのC末端側モチーフ配列と、デハイドリン固有のリジンモチーフ配列を有することが確認された。ペプシン消化性を検討した結果、16kDaペプシン消化耐性ポリペプチドの生成が見られた。","subitem_description_type":"Other"}]},"item_10002_identifier_registration":{"attribute_name":"ID登録","attribute_value_mlt":[{"subitem_identifier_reg_text":"10.24514/00002944","subitem_identifier_reg_type":"JaLC"}]},"item_10002_publisher_8":{"attribute_name":"出版者","attribute_value_mlt":[{"subitem_publisher":"農業・食品産業技術総合研究機構"}]},"item_10002_relation_14":{"attribute_name":"DOI","attribute_value_mlt":[{"subitem_relation_type":"isIdenticalTo","subitem_relation_type_id":{"subitem_relation_type_id_text":"10.24514/00002944","subitem_relation_type_select":"DOI"}}]},"item_10002_source_id_9":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"0301-9780","subitem_source_identifier_type":"ISSN"}]},"item_10002_version_type_20":{"attribute_name":"著者版フラグ","attribute_value_mlt":[{"subitem_version_resource":"http://purl.org/coar/version/c_970fb48d4fbd8a85","subitem_version_type":"VoR"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"門間, 美千子"},{"creatorName":"モンマ, ミチコ","creatorNameLang":"ja-Kana"},{"creatorName":"MONMA, Michiko","creatorNameLang":"en"}],"nameIdentifiers":[{},{},{}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2019-10-08"}],"displaytype":"detail","filename":"nfri_report_No79p35-39p.pdf","filesize":[{"value":"1.2 MB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"nfri_report_No79p35-39p.pdf","url":"https://repository.naro.go.jp/record/3068/files/nfri_report_No79p35-39p.pdf"},"version_id":"6f51c79a-cee5-4f5e-96fc-3df015496fd8"}]},"item_keyword":{"attribute_name":"キーワード","attribute_value_mlt":[{"subitem_subject":"group 2 LEA protein","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"buckwheat","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"16-kDa pepsin-resistant protein","subitem_subject_language":"en","subitem_subject_scheme":"Other"}]},"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":"Purification of Dehydrin Protein from Buckwheat Seed (Fagopyrum esculentum cv. Kitawase)","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"Purification of Dehydrin Protein from Buckwheat Seed (Fagopyrum esculentum cv. Kitawase)"},{"subitem_title":"Purification of Dehydrin Protein from Buckwheat Seed (Fagopyrum esculentum cv. Kitawase)","subitem_title_language":"en"}]},"item_type_id":"10002","owner":"12","path":["402"],"pubdate":{"attribute_name":"公開日","attribute_value":"2019-12-20"},"publish_date":"2019-12-20","publish_status":"0","recid":"3068","relation_version_is_last":true,"title":["Purification of Dehydrin Protein from Buckwheat Seed (Fagopyrum esculentum cv. Kitawase)"],"weko_creator_id":"12","weko_shared_id":12},"updated":"2023-05-15T15:52:04.779515+00:00"}