WEKO3
AND
アイテム
{"_buckets": {"deposit": "7a10eedd-2577-4709-a436-d298483b3b5b"}, "_deposit": {"id": "10598", "owners": [], "pid": {"revision_id": 0, "type": "depid", "value": "10598"}, "status": "published"}, "_oai": {"id": "oai:soar-ir.repo.nii.ac.jp:00010598"}, "item_6_alternative_title_1": {"attribute_name": "\u305d\u306e\u4ed6\uff08\u5225\u8a00\u8a9e\u7b49\uff09\u306e\u30bf\u30a4\u30c8\u30eb", "attribute_value_mlt": [{"subitem_alternative_title": "\u30da\u30d7\u30c1\u30c9\u5408\u6210\u307e\u305f\u306f\uff3a(\u30d9\u30f3\u30b8\u30eb\u30aa\u30ad\u30b7\u30ab\u30eb\u30dc\u30cb\u30eb\uff09 : \u30a2\u30df\u30ce\u9178\u30a8\u30b9\u30c6\u30eb\u52a0\u6c34\u5206\u89e3\u306b\u304a\u3051\u308b\uff12\uff0c\uff13\u306e\u30d7\u30ed\u30c6\u30a2\u30fc\u30bc\u306e\u5fae\u74b0\u5883\u3078\u306e\uff4e-\u30a2\u30eb\u30b3\u30fc\u30eb\u52b9\u679c\u306e\u591a\u69d8\u6027"}]}, "item_6_biblio_info_6": {"attribute_name": "\u66f8\u8a8c\u60c5\u5831", "attribute_value_mlt": [{"bibliographicIssueDates": {"bibliographicIssueDate": "1995-12-31", "bibliographicIssueDateType": "Issued"}, "bibliographicIssueNumber": "1-2", "bibliographicPageEnd": "22", "bibliographicPageStart": "15", "bibliographicVolumeNumber": "32", "bibliographic_titles": [{"bibliographic_title": "\u4fe1\u5dde\u5927\u5b66\u8fb2\u5b66\u90e8\u7d00\u8981"}]}]}, "item_6_description_20": {"attribute_name": "\u6284\u9332", "attribute_value_mlt": [{"subitem_description": "To investigate the interaction of proteases (thermolysin, \u03b1-chymotrypsin, papain and pepsin) with organic solvent molecules, buffer systems in which n-alcohols were dissolved as to make a one-phase medium were used in the case of peptide synthesis or Z-amino acid hydrolysis as model reactions. The chain length of n-alcohols gave different characteristics of the effective patterns to the enzymes, and also each protease was affected in different modes of effective profiles by n-alcohols. Activity of \u03b1-chymotrypsin was increased by n-alcohols higher than n-hexanol grdually with increase of their concentration just over the saturation to the buffer. The activation was proposed to be non-essential by kinetics. Meanwhile, n-pentanol to \u03b1-chymotrypsin showed to be an uncompetitive inhibitor.", "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": "\u4fe1\u5dde\u5927\u5b66\u8fb2\u5b66\u90e8\u7d00\u8981. 32(1-2): 15-22 (1995)", "subitem_description_type": "Other"}]}, "item_6_publisher_4": {"attribute_name": "\u51fa\u7248\u8005", "attribute_value_mlt": [{"subitem_publisher": "\u4fe1\u5dde\u5927\u5b66\u8fb2\u5b66\u90e8"}]}, "item_6_select_64": {"attribute_name": "\u8457\u8005\u7248\u30d5\u30e9\u30b0", "attribute_value_mlt": [{"subitem_select_item": "publisher"}]}, "item_6_source_id_35": {"attribute_name": "ISSN", "attribute_value_mlt": [{"subitem_source_identifier": "0583-0621", "subitem_source_identifier_type": "ISSN"}]}, "item_6_source_id_39": {"attribute_name": "NII ISSN", "attribute_value_mlt": [{"subitem_source_identifier": "0583-0621", "subitem_source_identifier_type": "ISSN"}]}, "item_6_source_id_40": {"attribute_name": "\u66f8\u8a8c\u30ec\u30b3\u30fc\u30c9ID", "attribute_value_mlt": [{"subitem_source_identifier": "AN00121352", "subitem_source_identifier_type": "NCID"}]}, "item_6_text_66": {"attribute_name": "sortkey", "attribute_value_mlt": [{"subitem_text_value": "03"}]}, "item_creator": {"attribute_name": "\u8457\u8005", "attribute_type": "creator", "attribute_value_mlt": [{"creatorNames": [{"creatorName": "Sato, K"}], "nameIdentifiers": [{"nameIdentifier": "33491", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "Tadasa, K"}], "nameIdentifiers": [{"nameIdentifier": "33492", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "Kayahara, H"}], "nameIdentifiers": [{"nameIdentifier": "33493", "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": "2015-09-25"}], "displaytype": "detail", "download_preview_message": "", "file_order": 0, "filename": "v32_03.pdf", "filesize": [{"value": "345.3 kB"}], "format": "application/pdf", "future_date_message": "", "is_thumbnail": false, "licensetype": "license_free", "mimetype": "application/pdf", "size": 345300.0, "url": {"label": "v32_03.pdf", "url": "https://soar-ir.repo.nii.ac.jp/record/10598/files/v32_03.pdf"}, "version_id": "de454218-236c-4e60-99b5-dc7e5cbf405b"}]}, "item_keyword": {"attribute_name": "\u30ad\u30fc\u30ef\u30fc\u30c9", "attribute_value_mlt": [{"subitem_subject": "protease", "subitem_subject_scheme": "Other"}, {"subitem_subject": "microenvironment", "subitem_subject_scheme": "Other"}, {"subitem_subject": "thermolysin", "subitem_subject_scheme": "Other"}, {"subitem_subject": "\u03b1-chymotrypsin", "subitem_subject_scheme": "Other"}, {"subitem_subject": "papain", "subitem_subject_scheme": "Other"}, {"subitem_subject": "pepsin", "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": "Variety of Effect of n-Alcohols on Microenvironment of Some Proteases in Peptide Synthesis or Z (N-Benzyloxycarbonyl) : Amino Acid Ester Hydrolysis", "item_titles": {"attribute_name": "\u30bf\u30a4\u30c8\u30eb", "attribute_value_mlt": [{"subitem_title": "Variety of Effect of n-Alcohols on Microenvironment of Some Proteases in Peptide Synthesis or Z (N-Benzyloxycarbonyl) : Amino Acid Ester Hydrolysis"}]}, "item_type_id": "6", "owner": "1", "path": ["1016/1018/1019/1039"], "permalink_uri": "http://hdl.handle.net/10091/845", "pubdate": {"attribute_name": "\u516c\u958b\u65e5", "attribute_value": "2007-12-28"}, "publish_date": "2007-12-28", "publish_status": "0", "recid": "10598", "relation": {}, "relation_version_is_last": true, "title": ["Variety of Effect of n-Alcohols on Microenvironment of Some Proteases in Peptide Synthesis or Z (N-Benzyloxycarbonyl) : Amino Acid Ester Hydrolysis"], "weko_shared_id": null}
Variety of Effect of n-Alcohols on Microenvironment of Some Proteases in Peptide Synthesis or Z (N-Benzyloxycarbonyl) : Amino Acid Ester Hydrolysis
http://hdl.handle.net/10091/845
0adb3600-9355-43b3-9843-8056e0c08487
名前 / ファイル | ライセンス | アクション | |
---|---|---|---|
![]() |
|
Item type | 学術雑誌論文 / Journal Article(1) | |||||
---|---|---|---|---|---|---|
公開日 | 2007-12-28 | |||||
タイトル | ||||||
タイトル | Variety of Effect of n-Alcohols on Microenvironment of Some Proteases in Peptide Synthesis or Z (N-Benzyloxycarbonyl) : Amino Acid Ester Hydrolysis | |||||
言語 | ||||||
言語 | eng | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | protease | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | microenvironment | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | thermolysin | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | α-chymotrypsin | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | papain | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | pepsin | |||||
資源タイプ | ||||||
資源 | http://purl.org/coar/resource_type/c_6501 | |||||
タイプ | journal article | |||||
その他(別言語等)のタイトル | ||||||
その他のタイトル | ペプチド合成またはZ(ベンジルオキシカルボニル) : アミノ酸エステル加水分解における2,3のプロテアーゼの微環境へのn-アルコール効果の多様性 | |||||
著者 |
Sato, K
× Sato, K× Tadasa, K× Kayahara, H |
|||||
出版者 | ||||||
出版者 | 信州大学農学部 | |||||
引用 | ||||||
内容記述タイプ | Other | |||||
内容記述 | 信州大学農学部紀要. 32(1-2): 15-22 (1995) | |||||
書誌情報 |
信州大学農学部紀要 巻 32, 号 1-2, p. 15-22, 発行日 1995-12-31 |
|||||
抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | To investigate the interaction of proteases (thermolysin, α-chymotrypsin, papain and pepsin) with organic solvent molecules, buffer systems in which n-alcohols were dissolved as to make a one-phase medium were used in the case of peptide synthesis or Z-amino acid hydrolysis as model reactions. The chain length of n-alcohols gave different characteristics of the effective patterns to the enzymes, and also each protease was affected in different modes of effective profiles by n-alcohols. Activity of α-chymotrypsin was increased by n-alcohols higher than n-hexanol grdually with increase of their concentration just over the saturation to the buffer. The activation was proposed to be non-essential by kinetics. Meanwhile, n-pentanol to α-chymotrypsin showed to be an uncompetitive inhibitor. | |||||
資源タイプ(コンテンツの種類) | ||||||
内容記述タイプ | Other | |||||
内容記述 | Article | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 0583-0621 | |||||
書誌レコードID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AN00121352 |