{"created":"2023-06-19T08:46:09.329500+00:00","id":4890,"links":{},"metadata":{"_buckets":{"deposit":"69125a67-1d24-409d-85b5-73d633d0f899"},"_deposit":{"created_by":14,"id":"4890","owners":[14],"pid":{"revision_id":0,"type":"depid","value":"4890"},"status":"published"},"_oai":{"id":"oai:kpu.repo.nii.ac.jp:00004890","sets":["47:273:415"]},"author_link":["8049","8050","7646"],"control_number":"4890","item_1696926521561":{"attribute_name":"その他（別言語等）","attribute_value_mlt":[{"subitem_alternative_title":"牛乳のκ- カゼインに関する研究 V : 化学修飾(農芸化学部門)","subitem_alternative_title_language":"ja"}]},"item_3_biblio_info_12":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"1971-10-15","bibliographicIssueDateType":"Issued"},"bibliographicPageEnd":"154","bibliographicPageStart":"145","bibliographicVolumeNumber":"23","bibliographic_titles":[{"bibliographic_title":"京都府立大學學術報告. 農學","bibliographic_titleLang":"ja"},{"bibliographic_title":"The scientific reports of Kyoto Prefectural University. Agriculture","bibliographic_titleLang":"en"}]}]},"item_3_description_10":{"attribute_name":"抄録(日)","attribute_value_mlt":[{"subitem_description":"κ-カゼインのアミノ基, カルボキシル基, SH基, チロシン, トリプトフアン, リジン, セリン, ヒスチジン, アルギニン, およびメチオニンを種々の方法で化学修飾し, それらがα_S-カゼイン安定化作用に及ぼす影響について調べた。今回の修飾反応条件であるpH7&acd;9においてはκ-カゼインはじゅうぶんに解離していないため, 反応基がκ-カゼイン複合体の表面に位置しているかどうかによって反応速度, ひいては修飾率が大きく左右された。アミノ基とカルボキシル基を修飾するとほぼ完全に安定化作用が消失し, ヒスチジンとチロシンの修飾も顕著な安定化力低下をもたらした。また, 還元してより低分子化すると未修飾κ-カゼインより安定化力が高まった。その他のアミノ酸残基の修飾はα_S-カゼインの安定化にほとんど無関係であった。焦点電気泳動による分析で, 6M尿素中においてκ-カゼインの等電点がpH5より酸性側へ移ると急にα_S-カゼインに対する安定化作用が失われることが判明した。デンプンゲル電気泳動によりκ-カゼインの化学修飾は分子電荷のみならず分子の大きさも変化させることが判明し, 特にセリン, ヒステジンそれにチロシンを修飾したものは会合が進み, 他方アミノ基とSH基を修飾したκ-カゼインはより小さい分子へ解離した。","subitem_description_language":"ja","subitem_description_type":"Other"}]},"item_3_description_11":{"attribute_name":"抄録(英)","attribute_value_mlt":[{"subitem_description":"κ-Casein was chemically modified in various ways. Modified groups include; NH_2 group, COOH group, tyrosine, tryptophan, lysine, SH group, serine, histidine, arginine and methionine. These groups and residues were not completely modified, probably because κ-casein was not dissociated into single molecules under the conditions used. Normally κ-casein has an S_<20,W> of about 14,which decreases to about 3 when dispersed by alkali or urea. Modification of NH_2 and COOH groups resulted in almost complete loss of the stabilization ability. Modification of histidine and tyrosine fairly well promoted a decrease in this function. Reduced κ-casein stabilized interestingly more α_S-casein than native κ-casein did. Modification of other amino acids had little effect on the stabilization ability. Results of isoelectric focusing indicate that κ-casein was unable to maintain its stabilization function when its isoelectric point in 6M urea moved toward acidic side beyond pH5.0. Six components of reduced κ-casein were clearly separated by isoelectric focusing in 6M urea. We observed that components with isoelectric points at the neutral side were most susceptible to modification. These components seem to occupy the surface of the κ-casein complex. Chemical modification was shown to result not only in changes in molecular charge, but in changes in molecular size.","subitem_description_language":"en","subitem_description_type":"Other"}]},"item_3_source_id_1":{"attribute_name":"雑誌書誌ID","attribute_value_mlt":[{"subitem_source_identifier":"AN00062275","subitem_source_identifier_type":"NCID"}]},"item_3_source_id_20":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"00757373","subitem_source_identifier_type":"PISSN"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"三好, 正満","creatorNameLang":"ja"},{"creatorName":"ミヨシ, マサミツ","creatorNameLang":"ja-Kana"},{"creatorName":"Miyoshi, Masamitsu","creatorNameLang":"en"}],"familyNames":[{},{},{}],"givenNames":[{},{},{}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"伊吹, 文男","creatorNameLang":"ja"},{"creatorName":"イブキ, フミオ","creatorNameLang":"ja-Kana"},{"creatorName":"Ibuki, Fumio","creatorNameLang":"en"}],"familyNames":[{},{},{}],"givenNames":[{},{},{}],"nameIdentifiers":[{}]},{"creatorAffiliations":[{"affiliationNameIdentifiers":[],"affiliationNames":[{"affiliationName":""}]}],"creatorNames":[{"creatorName":"金森, 正雄","creatorNameLang":"ja"},{"creatorName":"カナモリ, マサオ","creatorNameLang":"ja-Kana"},{"creatorName":"Kanamori, Masao","creatorNameLang":"en"}],"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":"2017-02-20"}],"displaytype":"detail","filename":"KJ00000078889.pdf","filesize":[{"value":"849.7 kB"}],"format":"application/pdf","mimetype":"application/pdf","url":{"label":"KJ00000078889.pdf","url":"https://kpu.repo.nii.ac.jp/record/4890/files/KJ00000078889.pdf"},"version_id":"529915be-60fb-4da3-bd33-e7bfbd3bf16b"}]},"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"}]},"item_title":"Studies on κ-Casein of Bovine Milk V : Chemical modification of κ-casein (Agricultural Chemistry)","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"Studies on κ-Casein of Bovine Milk V : Chemical modification of κ-casein (Agricultural Chemistry)","subitem_title_language":"en"}]},"item_type_id":"3","owner":"14","path":["415"],"pubdate":{"attribute_name":"PubDate","attribute_value":"2017-02-20"},"publish_date":"2017-02-20","publish_status":"0","recid":"4890","relation_version_is_last":true,"title":["Studies on κ-Casein of Bovine Milk V : Chemical modification of κ-casein (Agricultural Chemistry)"],"weko_creator_id":"14","weko_shared_id":-1},"updated":"2024-04-24T06:16:28.686275+00:00"}