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  1. 050 医学部, 大学院医学系研究科 (Faculty&Graduate School of Medicine)
  2. 0502 紀要・刊行物
  3. 05022 医療技術短期大学部紀要
  4. Vol. 27

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
Name / File License Actions
Allied_Med27_06.pdf Allied_Med27_06.pdf (592.3 kB)
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 Variantrlbrinogen
キーワード
主題 ‘A’polymerization site
キーワード
主題 ‘a’polymerization site
キーワード
主題 D-E binding
キーワード
主題 変異フィブリノゲン
キーワード
主題 ‘A’重合反応基
キーワード
主題 ‘a’重合反応基
キーワード
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

WEKO 16559

寺澤, 文子
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田中, 仁

× 田中, 仁

WEKO 16560

田中, 仁
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廣田(川戸洞), 雅子

× 廣田(川戸洞), 雅子

WEKO 16561

廣田(川戸洞), 雅子
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石川, 伸介

× 石川, 伸介

WEKO 16562

石川, 伸介
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奥村, 伸生

× 奥村, 伸生

WEKO 16563

奥村, 伸生
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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
著者版フラグ
値 publisher
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