{"created":"2023-07-27T06:44:38.294199+00:00","id":34933,"links":{},"metadata":{"_buckets":{"deposit":"3fc14776-5a88-40d9-89e8-eb2177efc025"},"_deposit":{"created_by":3,"id":"34933","owners":[3],"pid":{"revision_id":0,"type":"depid","value":"34933"},"status":"published"},"_oai":{"id":"oai:kanazawa-u.repo.nii.ac.jp:00034933","sets":["2812:2813:2845"]},"author_link":["24670","58300","92297","24669","92296","433","49415","24666"],"item_9_biblio_info_8":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"1989-03-01","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"1988","bibliographicPageStart":"50p.","bibliographicVolumeNumber":"1987","bibliographic_titles":[{"bibliographic_title":"昭和63(1988)年度 科学研究費補助金 一般研究(B) 研究成果報告書"},{"bibliographic_title":"1988 Fiscal Year Final Research Report","bibliographic_titleLang":"en"}]}]},"item_9_creator_33":{"attribute_name":"著者別表示","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{}],"nameIdentifiers":[{},{}]},{"creatorNames":[{}],"nameIdentifiers":[{},{}]},{"creatorNames":[{}],"nameIdentifiers":[{},{}]},{"creatorNames":[{}],"nameIdentifiers":[{},{}]}]},"item_9_description_21":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"ヘモグロビン(Hb)分子において(F8)、および遠位(E7)ヒスチジン(His)はヘムの酸化を防ぐためにも、協同的リガンド結合のためにも重要である。HbMはこれらのHisの1つがチロシン(Tyr)におきかわった異常血色素で、そのヘムは通常酸化した状態にある。HbMを有する人は、明瞭はチアノーゼを呈するが、HbM Saskatoon(Sas)(βE7His→Tyr)を有する人は、他のHbM症(HbM Iwate,αF8His→Tyr;HbM Boston,αE7His→Tyr;HbM Hyde Park,βF8His→Tyr)に較べてチアノーゼが弱い。何故このようにHbMの種類によって症状が異なるかを明らかにするため、まず異常鎖の赤血球のメトHb還元酵素による還元性を調べ、次に異常鎖の構造を共鳴ラマン(RR)、電子スピン共鳴(ESR)分光法で調べた。 嫌気条件では、HbM Sasの異常鎖はヒト赤血球から精製したNADH-メトHb還元酵素によって、正常Hbのメト型とほぼ同速度で還元されたが、他のHbMの異常鎖は還元されなかった。事実、最近我々はHbM Sas症患者新鮮血においては、異常鎖の半分以上は還元型で存在することをみつけた。 共鳴ラマンスペクトルでは、4種のTyr置換型HbMは、いずれもFe-tyrosinate蛋白としての指紋バンド(1600、1500、1270cm^<-1>)を示し、Fe-tyrの結合は、HbM Sasで一番弱かった。Fe-ポリフィリンの振動モードでみると、HbM Sasの異常鎖のみが6配位型(ヘム鉄はF8HisとE7Tyrの両方が結合)で、他のHbMでは5配位型(置換Tyrとのみ強く結合)の軸配位をとっていることが判明した。この相違が還元性の違いの原因となっているのであろう。 一方、異常鎖を還元してやると、一酸化炭素(CO)と結合できるようになる。そこで、異常鎖のリガンド結合性を共鳴ラマン、赤外、^<13>C-NMR分光法で調べ、改めて正常Hbにおける近位および遠位Hisの役割について検討した。","subitem_description_type":"Abstract"},{"subitem_description":"In the hemoglobin (Hb) molecule, the proximal and distal histidines are the most important for preventing the ferrous heme from oxidation and for the cooperative ligand binding. Hbs M are mutant hemoglobins, one of these histidines of which is replaced with tyrosine, and their hemes are stabilized usually in ferric state. Although patients of Hbs M show obvious cyanosis, only individuals with Hb M Saskatoon (beta E7 His-Tyr) have less cyanosis than those of the other Hbs M (Hb M Iwate, alpha F8 His-Tyr; Hb M Boston, alpha E7 His-Tyr; Hb M Hyde Park, beta F8 His-Tyr). In order to know why such symptoms for indivisuals with Hb M differ from each other, we have investigated the reducibility of abnormal chains of Hbs M by erythrocyte methemoglobin reductases and the structure of abnormal chains by using resonance Raman (RR), and electron spin resonance (ESR) spectrometry.\nUnder anaerobic conditions, abnormal chains of Hb M Saskatoon was reduced by methemoglobin reductases purified from huma n erythrocytes at almost the same rate as was metHb A. However, abnormal chains of the other Hbs M were scarcely reduced by these enzymes. In fact, we have found recently that more than half of the abnormal chains remained in ferrous state in the fresh bloods of individuals with Hb M Sastakoon.\nIn the RR spectra, all of four Hbs M exhibited the fingerprint bands for the Fe-tyrosinate proteins (1600, 1500 and 1270 cm^<-1>) and Fe-tyrosinate proteins (1600, 1500 and 1270 cm^<-1>) and Fe-tyrosinate stretching frequency in abnormal chain of Hb M Saskatoon was the lowest among them. However, only Hb M Saskatoon displayed the Raman spectral pattern of a six-coordinate heme for the abnormal subunit while others displayed that of a five-cooordinate heme. From these observations, it is concluded that the heme in abnormal chains of Hb M Iwate, Hb M Boston and Hb M Hyde Park, bind only with the substituted tyrosine, whereas that of Hb M Saskatoon binds weakly both the proximal histidine and the substituted tyrosine.\nAs abnormal chains of Hbs M can bind with carbonmonooxide (CO) after reduction by dithionite, we examined their unusual lignad binding properties by RR, infrared, and ^<13>C-NMR spectroscopy and discussed the role of the proximal and distal His on ligand binding properties in normal hemoglobin.","subitem_description_type":"Abstract"}]},"item_9_description_22":{"attribute_name":"内容記述","attribute_value_mlt":[{"subitem_description":"研究課題/領域番号:62480132, 研究期間(年度):1987–1988","subitem_description_type":"Other"},{"subitem_description":"出典：「ヘモグロビンMの分子病理学」研究成果報告書　課題番号62480132\n  (KAKEN：科学研究費助成事業データベース（国立情報学研究所）)\n　　　本文データは著者版報告書より作成","subitem_description_type":"Other"}]},"item_9_identifier_registration":{"attribute_name":"ID登録","attribute_value_mlt":[{"subitem_identifier_reg_text":"10.24517/00034920","subitem_identifier_reg_type":"JaLC"}]},"item_9_relation_28":{"attribute_name":"関連URI","attribute_value_mlt":[{"subitem_relation_type_id":{"subitem_relation_type_id_text":"https://kaken.nii.ac.jp/search/?qm=50135050","subitem_relation_type_select":"URI"}},{"subitem_relation_type_id":{"subitem_relation_type_id_text":"https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-62480132/","subitem_relation_type_select":"URI"}},{"subitem_relation_type_id":{"subitem_relation_type_id_text":"https://kaken.nii.ac.jp/report/KAKENHI-PROJECT-62480132/624801321988kenkyu_seika_hokoku_gaiyo/","subitem_relation_type_select":"URI"}}]},"item_9_version_type_25":{"attribute_name":"著者版フラグ","attribute_value_mlt":[{"subitem_version_resource":"http://purl.org/coar/version/c_ab4af688f83e57aa","subitem_version_type":"AM"}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2017-10-05"}],"displaytype":"detail","filename":"ME-PR-MAWATARI-K-kaken 1989-50p.pdf","filesize":[{"value":"1.4 MB"}],"format":"application/pdf","licensetype":"license_11","mimetype":"application/pdf","url":{"label":"ME-PR-MAWATARI-K-kaken 1989-50p.pdf","url":"https://kanazawa-u.repo.nii.ac.jp/record/34933/files/ME-PR-MAWATARI-K-kaken 1989-50p.pdf"},"version_id":"ee7fa557-4ea1-4e6e-b4a2-de81bb551891"}]},"item_language":{"attribute_name":"言語","attribute_value_mlt":[{"subitem_language":"jpn"}]},"item_resource_type":{"attribute_name":"資源タイプ","attribute_value_mlt":[{"resourcetype":"research report","resourceuri":"http://purl.org/coar/resource_type/c_18ws"}]},"item_title":"ヘモグロビンMの分子病理学","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"ヘモグロビンMの分子病理学"},{"subitem_title":"Molecular pathlogy of Hemoglobin M","subitem_title_language":"en"}]},"item_type_id":"9","owner":"3","path":["2845"],"pubdate":{"attribute_name":"公開日","attribute_value":"2017-10-05"},"publish_date":"2017-10-05","publish_status":"0","recid":"34933","relation_version_is_last":true,"title":["ヘモグロビンMの分子病理学"],"weko_creator_id":"3","weko_shared_id":3},"updated":"2023-07-27T14:51:04.943784+00:00"}