{"_buckets": {"deposit": "4979c81f-a179-4983-bdfa-e540e9d85a61"}, "_deposit": {"id": "13455", "owners": [], "pid": {"revision_id": 0, "type": "depid", "value": "13455"}, "status": "published"}, "_oai": {"id": "oai:soar-ir.repo.nii.ac.jp:00013455"}, "item_6_biblio_info_6": {"attribute_name": "\u66f8\u8a8c\u60c5\u5831", "attribute_value_mlt": [{"bibliographicIssueDates": {"bibliographicIssueDate": "2000", "bibliographicIssueDateType": "Issued"}, "bibliographicIssueNumber": "1", "bibliographicPageEnd": "112", "bibliographicPageStart": "105", "bibliographicVolumeNumber": "157", "bibliographic_titles": [{"bibliographic_title": "Plant Science"}]}]}, "item_6_description_20": {"attribute_name": "\u6284\u9332", "attribute_value_mlt": [{"subitem_description": "The enzyme UDP-glucose: hydroxycoumarin 7-O-glucosyltransferase (CGTase), which catalyzes the formation of scopolin from scopoletin, was purified approximately 1200-fold from a culture of 2,4-D-treated tobacco cells (Nicotiana tabacum L. cv. Bright Yellow T-13) with a yield of 7%. Purification to apparent homogeneity, as judged by SDS-PAGE, was achieved by sequential anion-exchange chromatography, hydroxyapatite chromatography, gel filtration, a second round of anion-exchange chromatography, and affinity chromatography on UDP-glucuronic acid agarose. The purified enzyme had a pH optimum of 7.5, an isoelectric point (pI) of 5.0, and a molecular mass of 49 kDa. The enzyme did not require metal cofactors for activity. Its activity was inhibited by Zn2+, Co2+ and Cu2+ ions, as well as by SH-blocking reagents. The K-m values for UDP-glucose, scopoletin and esculetin were 43, 150 and 25 mu M. respectively. A study of the initial rate of the reaction suggested that the reaction proceeded via a sequential mechanism. The purified enzyme preferred hydroxycoumarins as substrates but also exhibited significant activity with flavonoids. A database search using the amino terminus amino acid sequence of CGTase revealed strong homology to the amino acid sequences of other glucosyltransferases in plants.", "subitem_description_type": "Abstract"}]}, "item_6_description_30": {"attribute_name": "\u8cc7\u6e90\u30bf\u30a4\u30d7\uff08\u30b3\u30f3\u30c6\u30f3\u30c4\u306e\u7a2e\u985e\uff09", "attribute_value_mlt": [{"subitem_description": "Article", "subitem_description_type": "Other"}]}, "item_6_description_31": {"attribute_name": "\u30d5\u30a9\u30fc\u30de\u30c3\u30c8\uff1amime\u30bf\u30a4\u30d7", "attribute_value_mlt": [{"subitem_description": "application/pdf", "subitem_description_type": "Other"}]}, "item_6_description_5": {"attribute_name": "\u5f15\u7528", "attribute_value_mlt": [{"subitem_description": "Plant Science. 157(1):105-112 (2000)", "subitem_description_type": "Other"}]}, "item_6_link_3": {"attribute_name": "\u4fe1\u5dde\u5927\u5b66\u7814\u7a76\u8005\u7dcf\u89a7\u3078\u306e\u30ea\u30f3\u30af", "attribute_value_mlt": [{"subitem_link_text": "Taguchi, G", "subitem_link_url": "http://soar-rd.shinshu-u.ac.jp/profile/ja.uCDpjekV.html"}, {"subitem_link_text": "Hayashida, N", "subitem_link_url": "http://soar-rd.shinshu-u.ac.jp/profile/ja.HVfmjekV.html"}, {"subitem_link_text": "Shimosaka, M", "subitem_link_url": "http://soar-rd.shinshu-u.ac.jp/profile/ja.ZekmjekV.html"}]}, "item_6_link_67": {"attribute_name": "WoS", "attribute_value_mlt": [{"subitem_link_text": "Web of Science", "subitem_link_url": "http://gateway.isiknowledge.com/gateway/Gateway.cgi?\u0026GWVersion=2\u0026SrcAuth=ShinshuUniv\u0026SrcApp=ShinshuUniv\u0026DestLinkType=FullRecord\u0026DestApp=WOS\u0026KeyUT=000088553500011"}]}, "item_6_publisher_4": {"attribute_name": "\u51fa\u7248\u8005", "attribute_value_mlt": [{"subitem_publisher": "Elsevier"}]}, "item_6_relation_46": {"attribute_name": "\u4ed6\u306e\u8cc7\u6e90\u3068\u306e\u95a2\u4fc2\uff1aURI", "attribute_value_mlt": [{"subitem_relation_name": [{"subitem_relation_name_text": "http://www.elsevier.com/locate/plantsci"}], "subitem_relation_type_id": {"subitem_relation_type_id_text": "http://www.elsevier.com/locate/plantsci", "subitem_relation_type_select": "URI"}}]}, "item_6_relation_47": {"attribute_name": "PubMed", "attribute_value_mlt": [{"subitem_relation_name": [{"subitem_relation_name_text": "10940474"}], "subitem_relation_type_id": {"subitem_relation_type_id_text": "http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?CMD=search\u0026DB=pubmed\u0026term=10940474", "subitem_relation_type_select": "PMID"}}]}, "item_6_relation_48": {"attribute_name": "DOI", "attribute_value_mlt": [{"subitem_relation_name": [{"subitem_relation_name_text": "10.1016/S0168-9452(00)00270-3"}], "subitem_relation_type_id": {"subitem_relation_type_id_text": "http://dx.doi.org/10.1016/S0168-9452(00)00270-3", "subitem_relation_type_select": "DOI"}}]}, "item_6_select_64": {"attribute_name": "\u8457\u8005\u7248\u30d5\u30e9\u30b0", "attribute_value_mlt": [{"subitem_select_item": "author"}]}, "item_6_source_id_35": {"attribute_name": "ISSN", "attribute_value_mlt": [{"subitem_source_identifier": "0168-9452", "subitem_source_identifier_type": "ISSN"}]}, "item_6_source_id_39": {"attribute_name": "NII ISSN", "attribute_value_mlt": [{"subitem_source_identifier": "0168-9452", "subitem_source_identifier_type": "ISSN"}]}, "item_6_source_id_40": {"attribute_name": "\u66f8\u8a8c\u30ec\u30b3\u30fc\u30c9ID", "attribute_value_mlt": [{"subitem_source_identifier": "AA10531279", "subitem_source_identifier_type": "NCID"}]}, "item_6_text_69": {"attribute_name": "wosonly authkey", "attribute_value_mlt": [{"subitem_text_value": "Nicotiana tabacum L. cv Bright Yellow; glucosyltransferase; scopoletin; esculetin; flavonoid"}]}, "item_6_text_70": {"attribute_name": "wosonly keywords", "attribute_value_mlt": [{"subitem_text_value": "BETA-D-GLUCOSYLTRANSFERASE; SALICYLIC-ACID; METHYL JASMONATE; ACCUMULATION; ELICITOR; ENZYMES; CLONING; GENE"}]}, "item_6_textarea_68": {"attribute_name": "wosonly abstract", "attribute_value_mlt": [{"subitem_textarea_value": "The enzyme UDP-glucose: hydroxycoumarin 7-O-glucosyltransferase (CGTase), which catalyzes the formation of scopolin from scopoletin, was purified approximately 1200-fold from a culture of 2,4-D-treated tobacco cells (Nicotiana tabacum L. cv. Bright Yellow T-13) with a yield of 7%. Purification to apparent homogeneity, as judged by SDS-PAGE, was achieved by sequential anion-exchange chromatography, hydroxyapatite chromatography, gel filtration, a second round of anion-exchange chromatography, and affinity chromatography on UDP-glucuronic acid agarose. The purified enzyme had a pH optimum of 7.5, an isoelectric point (pI) of 5.0, and a molecular mass of 49 kDa. The enzyme did not require metal cofactors for activity. Its activity was inhibited by Zn2+, Co2+ and Cu2+ ions, as well as by SH-blocking reagents. The K-m values for UDP-glucose, scopoletin and esculetin were 43, 150 and 25 mu M. respectively. A study of the initial rate of the reaction suggested that the reaction proceeded via a sequential mechanism. The purified enzyme preferred hydroxycoumarins as substrates but also exhibited significant activity with flavonoids. A database search using the amino terminus amino acid sequence of CGTase revealed strong homology to the amino acid sequences of other glucosyltransferases in plants."}]}, "item_creator": {"attribute_name": "\u8457\u8005", "attribute_type": "creator", "attribute_value_mlt": [{"creatorNames": [{"creatorName": "Taguchi,  G"}], "nameIdentifiers": [{"nameIdentifier": "41014", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "Imura,  H"}], "nameIdentifiers": [{"nameIdentifier": "41015", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "Maeda,  Y"}], "nameIdentifiers": [{"nameIdentifier": "41016", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "Kodaira,  R"}], "nameIdentifiers": [{"nameIdentifier": "41017", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "Hayashida,  N"}], "nameIdentifiers": [{"nameIdentifier": "41018", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "Shimosaka,  M"}], "nameIdentifiers": [{"nameIdentifier": "41019", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "Okazaki,  M"}], "nameIdentifiers": [{"nameIdentifier": "41020", "nameIdentifierScheme": "WEKO"}]}]}, "item_files": {"attribute_name": "\u30d5\u30a1\u30a4\u30eb\u60c5\u5831", "attribute_type": "file", "attribute_value_mlt": [{"accessrole": "open_date", "date": [{"dateType": "Available", "dateValue": "2015-09-28"}], "displaytype": "detail", "download_preview_message": "", "file_order": 0, "filename": "Plant Sci 2000.pdf", "filesize": [{"value": "1.3 MB"}], "format": "application/pdf", "future_date_message": "", "is_thumbnail": false, "licensetype": "license_free", "mimetype": "application/pdf", "size": 1300000.0, "url": {"label": "Plant Sci 2000.pdf", "url": "https://soar-ir.repo.nii.ac.jp/record/13455/files/Plant Sci 2000.pdf"}, "version_id": "97b52b55-ab11-4e0c-a5b4-62de41cb230a"}]}, "item_keyword": {"attribute_name": "\u30ad\u30fc\u30ef\u30fc\u30c9", "attribute_value_mlt": [{"subitem_subject": "Nicotiana tabacum L. cv Bright Yellow", "subitem_subject_scheme": "Other"}, {"subitem_subject": "glucosyltransferase", "subitem_subject_scheme": "Other"}, {"subitem_subject": "scopoletin", "subitem_subject_scheme": "Other"}, {"subitem_subject": "esculetin", "subitem_subject_scheme": "Other"}, {"subitem_subject": "flavonoid", "subitem_subject_scheme": "Other"}]}, "item_language": {"attribute_name": "\u8a00\u8a9e", "attribute_value_mlt": [{"subitem_language": "eng"}]}, "item_resource_type": {"attribute_name": "\u8cc7\u6e90\u30bf\u30a4\u30d7", "attribute_value_mlt": [{"resourcetype": "journal article", "resourceuri": "http://purl.org/coar/resource_type/c_6501"}]}, "item_title": "Purification and characterization of UDP-glucose: hydroxycoumarin 7-O-glucosyltransferase, with broad substrate specificity from tobacco cultured cells", "item_titles": {"attribute_name": "\u30bf\u30a4\u30c8\u30eb", "attribute_value_mlt": [{"subitem_title": "Purification and characterization of UDP-glucose: hydroxycoumarin 7-O-glucosyltransferase, with broad substrate specificity from tobacco cultured cells"}]}, "item_type_id": "6", "owner": "1", "path": ["1309/1310"], "permalink_uri": "http://hdl.handle.net/10091/10111", "pubdate": {"attribute_name": "\u516c\u958b\u65e5", "attribute_name_i18n": "\u516c\u958b\u65e5", "attribute_value": "2010-05-26"}, "publish_date": "2010-05-26", "publish_status": "0", "recid": "13455", "relation": {}, "relation_version_is_last": true, "title": ["Purification and characterization of UDP-glucose: hydroxycoumarin 7-O-glucosyltransferase, with broad substrate specificity from tobacco cultured cells"], "weko_shared_id": null}