{"created":"2023-05-15T09:41:16.088923+00:00","id":344,"links":{},"metadata":{"_buckets":{"deposit":"10d4c999-e2d6-443c-98c4-e6c3895d9c3c"},"_deposit":{"created_by":11,"id":"344","owners":[11],"pid":{"revision_id":0,"type":"depid","value":"344"},"status":"published"},"_oai":{"id":"oai:kagawa-u.repo.nii.ac.jp:00000344","sets":["13:40"]},"author_link":["1159"],"item_10006_date_granted_11":{"attribute_name":"学位授与年月日","attribute_value_mlt":[{"subitem_dategranted":"2018-12-26"}]},"item_10006_degree_grantor_9":{"attribute_name":"学位授与機関","attribute_value_mlt":[{"subitem_degreegrantor":[{"subitem_degreegrantor_language":"ja","subitem_degreegrantor_name":"香川大学"},{"subitem_degreegrantor_language":"en","subitem_degreegrantor_name":"Kagawa University"}],"subitem_degreegrantor_identifier":[{"subitem_degreegrantor_identifier_name":"16201","subitem_degreegrantor_identifier_scheme":"kakenhi"}]}]},"item_10006_degree_name_8":{"attribute_name":"学位名","attribute_value_mlt":[{"subitem_degreename":"博士（医学）","subitem_degreename_language":"ja"}]},"item_10006_description_7":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"Abstract\nThe human gut commensal Bacteroides fragilis produces sialidases that remove a terminal sialic acid from host-derived polysaccharides. Sialidase is considered to be involved in B. fragilis infection pathology. A native B. fragilis sialidase has been purified and characterized, and was shown to be post-translationally modified by glycosylation. However, the biochemical properties of recombinant B. fragilis sialidase expressed in a heterologous host remain uncharacterized. In this study, we examined the enzymatic properties of the 60-kDa sialidase NanH1 of B. fragilis YCH46, which was prepared as a recombinant protein (rNanH1) in Escherichia coli. In E. coli rNanH1 was expressed as inclusion bodies, which were separated from soluble proteins to allow solubilization of insoluble rNanH1 in a buffer containing 8 M urea and renaturation in refolding buffer containing 100 mM CaCl2 and 50 mM L-arginine. The specific activity of renatured rNanH1 measured using 4-methylumberiferyl-α-D-N-acetyl neuraminic acid as a substrate was 6.16 μmol/min/mg. The optimal pH of rNanH1 ranged from 5.0 to 5.5. The specific activity of rNanH1 was enhanced in the presence of calcium ions. rNanH1 preferentially hydrolyzed the sialyl α2,8 linkage and cleaved sialic acids from mucin and serum proteins (e.g., fetuin and transferrin) but not from α1-acid glycoprotein, which is similar to the previously observed biochemical properties for a native sialidase purified from B. fragilis SBT3182. The results and methods described in this study will be useful for preparing and characterizing recombinant proteins for other B. fragilis sialidase isoenzymes.","subitem_description_language":"en","subitem_description_type":"Abstract"}]},"item_10006_dissertation_number_12":{"attribute_name":"学位授与番号","attribute_value_mlt":[{"subitem_dissertationnumber":"甲第702号"}]},"item_10006_relation_15":{"attribute_name":"関連サイト","attribute_value_mlt":[{"subitem_relation_type":"isVersionOf","subitem_relation_type_id":{"subitem_relation_type_id_text":"https://doi.org/10.1016/j.anaerobe.2018.02.003","subitem_relation_type_select":"DOI"}},{"subitem_relation_type":"isIdenticalTo","subitem_relation_type_id":{"subitem_relation_type_id_text":"https://dl.ndl.go.jp/pid/11246014","subitem_relation_type_select":"URI"}}]},"item_10006_relation_22":{"attribute_name":"PubMed番号","attribute_value_mlt":[{"subitem_relation_type_id":{"subitem_relation_type_id_text":"29432848","subitem_relation_type_select":"PMID"}}]},"item_10006_relation_28":{"attribute_name":"論文ID（NAID）","attribute_value_mlt":[{"subitem_relation_type_id":{"subitem_relation_type_id_text":"500001323355","subitem_relation_type_select":"NAID"}}]},"item_10006_rights_13":{"attribute_name":"権利","attribute_value_mlt":[{"subitem_rights":"Copyright © 2018 Elsevier Ltd. All rights reserved.","subitem_rights_language":"en"},{"subitem_rights":"エルゼビア・ジャパンより、博士論文については、機関リポジトリでの公開可能確認済み。","subitem_rights_language":"ja"},{"subitem_rights":"Elsevier Japan has confirmed the publication possibility in the institutional repository about the doctoral thesis.","subitem_rights_language":"en"}]},"item_10006_text_30":{"attribute_name":"KEID","attribute_value_mlt":[{"subitem_text_value":"28573"}]},"item_10006_version_type_18":{"attribute_name":"著者版フラグ","attribute_value_mlt":[{"subitem_version_resource":"http://purl.org/coar/version/c_fa2ee174bc00049f","subitem_version_type":"P"}]},"item_access_right":{"attribute_name":"アクセス権","attribute_value_mlt":[{"subitem_access_right":"open access","subitem_access_right_uri":"http://purl.org/coar/access_right/c_abf2"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorAffiliations":[{"affiliationNameIdentifiers":[{"affiliationNameIdentifier":"","affiliationNameIdentifierScheme":"ISNI","affiliationNameIdentifierURI":"http://www.isni.org/isni/"}],"affiliationNames":[{"affiliationName":"","affiliationNameLang":"ja"}]}],"creatorNames":[{"creatorName":"Yamamoto, Takaaki","creatorNameLang":"en"},{"creatorName":"山本, 高成","creatorNameLang":"ja"},{"creatorName":"ヤマモト, タカアキ","creatorNameLang":"ja-Kana"}],"familyNames":[{},{},{}],"givenNames":[{},{},{}],"nameIdentifiers":[{},{}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2020-11-05"}],"displaytype":"detail","filename":"Med_A702.pdf","filesize":[{"value":"2.3 MB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"本文","objectType":"fulltext","url":"https://kagawa-u.repo.nii.ac.jp/record/344/files/Med_A702.pdf"},"version_id":"f25a0054-8cc2-4962-ad37-dc3793ec2607"},{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2020-11-05"}],"displaytype":"detail","filename":"Med_A702_abstract.pdf","filesize":[{"value":"79.4 kB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"内容の要旨","objectType":"abstract","url":"https://kagawa-u.repo.nii.ac.jp/record/344/files/Med_A702_abstract.pdf"},"version_id":"6df9b622-f4df-4476-a611-ca188ea9ca5c"},{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2020-11-05"}],"displaytype":"detail","filename":"Med_A702_result.pdf","filesize":[{"value":"408.7 kB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"審査の結果の要旨","objectType":"other","url":"https://kagawa-u.repo.nii.ac.jp/record/344/files/Med_A702_result.pdf"},"version_id":"3b7146f7-9cd6-4fc2-8eb0-7ba642349e04"}]},"item_keyword":{"attribute_name":"キーワード","attribute_value_mlt":[{"subitem_subject":"Bacteroides fragilis","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Sialidase","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Sialic acid","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Sialyl α2,8 linkage","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"Mucin","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":"doctoral thesis","resourceuri":"http://purl.org/coar/resource_type/c_db06"}]},"item_title":"Characterization of a recombinant Bacteroides fragilis sialidase expressed in Escherichia coli","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"Characterization of a recombinant Bacteroides fragilis sialidase expressed in Escherichia coli","subitem_title_language":"en"}]},"item_type_id":"10006","owner":"11","path":["40"],"pubdate":{"attribute_name":"PubDate","attribute_value":"2019-01-30"},"publish_date":"2019-01-30","publish_status":"0","recid":"344","relation_version_is_last":true,"title":["Characterization of a recombinant Bacteroides fragilis sialidase expressed in Escherichia coli"],"weko_creator_id":"11","weko_shared_id":-1},"updated":"2023-12-26T02:09:52.305135+00:00"}