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フイプリン重合反応におけるD-E (‘a-A’)結合異常の解析 : Dドメイン(‘a’)に変異を有するMatsumoto I (γ364Asp→His)とEドメイン(‘A’)に変異を有するMatsumoto V (Aα19Arg→Gly)の比較
http://hdl.handle.net/10091/5255
346359bd-7eb1-47d2-848f-0dd10ef82359
| 名前 / ファイル | ライセンス | アクション | |
|---|---|---|---|
Allied_Med27_06.pdf (592.3 kB)
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| Item type | 紀要論文 / Departmental Bulletin Paper(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2010-03-01 | |||||
| タイトル | ||||||
| タイトル | フイプリン重合反応におけるD-E (‘a-A’)結合異常の解析 : Dドメイン(‘a’)に変異を有するMatsumoto I (γ364Asp→His)とEドメイン(‘A’)に変異を有するMatsumoto V (Aα19Arg→Gly)の比較 | |||||
| 言語 | ||||||
| 言語 | jpn | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | Variantrlbrinogen | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | ‘A’polymerization site | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | ‘a’polymerization site | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | D-E binding | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | 変異フィブリノゲン | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | ‘A’重合反応基 | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | ‘a’重合反応基 | |||||
| キーワード | ||||||
| 主題Scheme | Other | |||||
| 主題 | D-E結合 | |||||
| 資源タイプ | ||||||
| 資源 | http://purl.org/coar/resource_type/c_6501 | |||||
| タイプ | departmental bulletin paper | |||||
| その他（別言語等）のタイトル | ||||||
| その他のタイトル | Functional analyses for D-E binding of fibrin polymerization -Functional comparison between Matsumoto I (γ364Asp→His) having impaired D domain (‘a’site) and Matsumoto V (Aα19Arg→Gly)having impaired E domain (‘A’site) | |||||
| 著者 |
寺澤, 文子
× 寺澤, 文子× 田中, 仁× 廣田(川戸洞), 雅子× 石川, 伸介× 奥村, 伸生 |
|||||
| 信州大学研究者総覧へのリンク | ||||||
| 氏名 | 奥村, 伸生 | |||||
| URL | http://soar-rd.shinshu-u.ac.jp/profile/ja.OVnmgCkh.html | |||||
| 出版者 | ||||||
| 出版者 | 信州大学医療技術短期大学部 | |||||
| 引用 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | 紀要 27: 57-66(2002) | |||||
| 書誌情報 |
紀要 巻 27, p. 57-66, 発行日 2002-02-28 |
|||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | Fibrinogen Matsumoto I (M・I)and V (M ･V) are dysfibrinogens which are heterozygous (Asp or His) at γ364 and heterozygous (Arg or Gly) at Aα19, respectively. γ364 and Aα19 have been demonstrated to be the most important residue in the so-called ‘a’site in the D domain and the ‘A’site in the E domain, respectively. Although the thrombin-catalyzed release of fibrinopeptide A from M･I and M･V was almost the same as that, from normal controls, their thrombin-catalyzed fibrin polymerization (TCFP) was markedly impaired as compared with normal fibrinogen. Furthermore, their reptilase-catalyzed fibrin polymerization (RCFP) was much more impaired than their TCFP. In particular, no significant RCFP was observed in the case of M・Ｉ. Taken together our observations suggest that, when the ‘Ａ’site is impaired in TCFP, ‘a-B’'binding of M･V may play a more important role, and when the ‘a’site is impaired, ‘b-A’and/or ‘b-Ｂ’interaction may not compensate for the polymerization of M･I. | |||||
| 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 | 0385-1982 | |||||
| 書誌レコードID | ||||||
| 収録物識別子タイプ | NCID | |||||
| 収録物識別子 | AN10402438 | |||||
