WEKO3
アイテム
{"_buckets": {"deposit": "f6995c1f-d12e-43de-819e-1869b5021d62"}, "_deposit": {"id": "38400", "owners": [], "pid": {"revision_id": 0, "type": "depid", "value": "38400"}, "status": "published"}, "_oai": {"id": "oai:tsukuba.repo.nii.ac.jp:00038400", "sets": ["306", "5287"]}, "item_5_biblio_info_6": {"attribute_name": "書誌情報", "attribute_value_mlt": [{"bibliographicIssueDates": {"bibliographicIssueDate": "2016", "bibliographicIssueDateType": "Issued"}, "bibliographicIssueNumber": "2", "bibliographicPageEnd": "125", "bibliographicPageStart": "116", "bibliographicVolumeNumber": "17", "bibliographic_titles": [{"bibliographic_title": "Current pharmaceutical biotechnology"}]}]}, "item_5_creator_3": {"attribute_name": "著者別名", "attribute_type": "creator", "attribute_value_mlt": [{"creatorNames": [{"creatorName": "白木, 賢太郎"}], "nameIdentifiers": [{"nameIdentifier": "79", "nameIdentifierScheme": "WEKO"}, {"nameIdentifier": "90334797", "nameIdentifierScheme": "e-Rad", "nameIdentifierURI": "https://nrid.nii.ac.jp/ja/nrid/1000090334797"}, {"nameIdentifier": "0000000710", "nameIdentifierScheme": "筑波大学研究者総覧", "nameIdentifierURI": "http://trios.tsukuba.ac.jp/researcher/0000000710"}]}]}, "item_5_description_4": {"attribute_name": "抄録", "attribute_value_mlt": [{"subitem_description": "Proteins are prone to inactivation in aqueous solutions because chemical modification and aggregation usually occur, particularly at high temperature. This review focuses on the recent advance in practical application with amine compounds that prevent the heat-induced inactivation and aggregation of proteins. Coexistence of amine solutes, typically diamines, polyamines, amino acid esters, and amidated amino acids decreases the heat-induced inactivation rate of proteins by one order of magnitude compared with that in the absence of additives under low concentrations of proteins at physiological pH. The amine compounds mainly suppress chemical modification, typically the β-elimination of disulfide bond and deamidation of asparagine side chain, thereby preventing heat-induced inactivation of proteins. Polyamines do not improve the refolding yield of proteins, owing to decrease in the solubility of unfolded proteins. In contrast, arginine is the most versatile additive for various situations, such as refolding of recombinant proteins, solubilized water-insoluble compounds, and prevention of nonspecific binding to solid surfaces; however, it is not always effective for preventing heat-induced aggregation. Amine compounds will be a key to prevent protein inactivation in solution additives.", "subitem_description_type": "Abstract"}]}, "item_5_publisher_27": {"attribute_name": "出版者", "attribute_value_mlt": [{"subitem_publisher": "Bentham Science Publishers"}]}, "item_5_relation_10": {"attribute_name": "PubMed番号", "attribute_value_mlt": [{"subitem_relation_type_id": {"subitem_relation_type_id_text": "26511979", "subitem_relation_type_select": "PMID"}}]}, "item_5_relation_11": {"attribute_name": "DOI", "attribute_value_mlt": [{"subitem_relation_type_id": {"subitem_relation_type_id_text": "10.2174/1389201017666151029110229", "subitem_relation_type_select": "DOI"}}]}, "item_5_rights_12": {"attribute_name": "権利", "attribute_value_mlt": [{"subitem_rights": "This article is available to download for free under the Open Access Plus program of Bentham Science in which the content is published under the creative commons license CC BY –NC –ND 4.0 "}]}, "item_5_select_15": {"attribute_name": "著者版フラグ", "attribute_value_mlt": [{"subitem_select_item": "publisher"}]}, "item_5_source_id_7": {"attribute_name": "ISSN", "attribute_value_mlt": [{"subitem_source_identifier": "1389-2010", "subitem_source_identifier_type": "ISSN"}]}, "item_5_source_id_9": {"attribute_name": "書誌レコードID", "attribute_value_mlt": [{"subitem_source_identifier": "AA11692444", "subitem_source_identifier_type": "NCID"}]}, "item_5_subject_20": {"attribute_name": "NIIサブジェクト", "attribute_value_mlt": [{"subitem_subject": "基礎工学・応用物理学 ", "subitem_subject_scheme": "Other"}]}, "item_creator": {"attribute_name": "著者", "attribute_type": "creator", "attribute_value_mlt": [{"creatorNames": [{"creatorName": "Shiraki, Kentaro"}], "nameIdentifiers": [{"nameIdentifier": "136623", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "Tomita, Shunsuke"}], "nameIdentifiers": [{"nameIdentifier": "136624", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "Inoue, Naoto"}], "nameIdentifiers": [{"nameIdentifier": "136625", "nameIdentifierScheme": "WEKO"}]}]}, "item_files": {"attribute_name": "ファイル情報", "attribute_type": "file", "attribute_value_mlt": [{"accessrole": "open_date", "date": [{"dateType": "Available", "dateValue": "2016-07-01"}], "displaytype": "detail", "download_preview_message": "", "file_order": 0, "filename": "CPB_17-2.pdf", "filesize": [{"value": "1.5 MB"}], "format": "application/pdf", "future_date_message": "", "is_thumbnail": false, "licensetype": "license_11", "mimetype": "application/pdf", "size": 1500000.0, "url": {"label": "CPB_17-2", "url": "https://tsukuba.repo.nii.ac.jp/record/38400/files/CPB_17-2.pdf"}, "version_id": "3721c414-30eb-4b33-a582-34776e6894ed"}]}, "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": "journal article", "resourceuri": "http://purl.org/coar/resource_type/c_6501"}]}, "item_title": "Small Amine Molecules: Solvent Design Toward Facile Improvement of Protein Stability Against Aggregation and Inactivation", "item_titles": {"attribute_name": "タイトル", "attribute_value_mlt": [{"subitem_title": "Small Amine Molecules: Solvent Design Toward Facile Improvement of Protein Stability Against Aggregation and Inactivation"}]}, "item_type_id": "5", "owner": "1", "path": ["306", "5287"], "permalink_uri": "http://hdl.handle.net/2241/00143069", "pubdate": {"attribute_name": "公開日", "attribute_value": "2016-07-01"}, "publish_date": "2016-07-01", "publish_status": "0", "recid": "38400", "relation": {}, "relation_version_is_last": true, "title": ["Small Amine Molecules: Solvent Design Toward Facile Improvement of Protein Stability Against Aggregation and Inactivation"], "weko_shared_id": 5}
Small Amine Molecules: Solvent Design Toward Facile Improvement of Protein Stability Against Aggregation and Inactivation
http://hdl.handle.net/2241/00143069
http://hdl.handle.net/2241/00143069af6e37f6-329a-4098-9403-30c92070c1ca
名前 / ファイル | ライセンス | アクション |
---|---|---|
CPB_17-2 (1.5 MB)
|
Item type | Journal Article(1) | |||||
---|---|---|---|---|---|---|
公開日 | 2016-07-01 | |||||
タイトル | ||||||
タイトル | Small Amine Molecules: Solvent Design Toward Facile Improvement of Protein Stability Against Aggregation and Inactivation | |||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源 | http://purl.org/coar/resource_type/c_6501 | |||||
タイプ | journal article | |||||
著者 |
Shiraki, Kentaro
× Shiraki, Kentaro× Tomita, Shunsuke× Inoue, Naoto |
|||||
著者別名 |
白木, 賢太郎
× 白木, 賢太郎 |
|||||
抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | Proteins are prone to inactivation in aqueous solutions because chemical modification and aggregation usually occur, particularly at high temperature. This review focuses on the recent advance in practical application with amine compounds that prevent the heat-induced inactivation and aggregation of proteins. Coexistence of amine solutes, typically diamines, polyamines, amino acid esters, and amidated amino acids decreases the heat-induced inactivation rate of proteins by one order of magnitude compared with that in the absence of additives under low concentrations of proteins at physiological pH. The amine compounds mainly suppress chemical modification, typically the β-elimination of disulfide bond and deamidation of asparagine side chain, thereby preventing heat-induced inactivation of proteins. Polyamines do not improve the refolding yield of proteins, owing to decrease in the solubility of unfolded proteins. In contrast, arginine is the most versatile additive for various situations, such as refolding of recombinant proteins, solubilized water-insoluble compounds, and prevention of nonspecific binding to solid surfaces; however, it is not always effective for preventing heat-induced aggregation. Amine compounds will be a key to prevent protein inactivation in solution additives. | |||||
書誌情報 |
Current pharmaceutical biotechnology 巻 17, 号 2, p. 116-125, 発行日 2016 |
|||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 1389-2010 | |||||
書誌レコードID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AA11692444 | |||||
PubMed番号 | ||||||
識別子タイプ | PMID | |||||
関連識別子 | 26511979 | |||||
DOI | ||||||
識別子タイプ | DOI | |||||
関連識別子 | 10.2174/1389201017666151029110229 | |||||
権利 | ||||||
権利情報 | This article is available to download for free under the Open Access Plus program of Bentham Science in which the content is published under the creative commons license CC BY –NC –ND 4.0 | |||||
著者版フラグ | ||||||
値 | publisher | |||||
出版者 | ||||||
出版者 | Bentham Science Publishers |