2024-03-28T14:18:53Z
https://soar-ir.repo.nii.ac.jp/oai
oai:soar-ir.repo.nii.ac.jp:00006860
2023-02-13T01:11:25Z
461:463:805:806
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
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)
寺澤, 文子
田中, 仁
廣田(川戸洞), 雅子
石川, 伸介
奥村, 伸生
Variantrlbrinogen
‘A’polymerization site
‘a’polymerization site
D-E binding
変異フィブリノゲン
‘A’重合反応基
‘a’重合反応基
D-E結合
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.
Article
紀要 27: 57-66(2002)
信州大学医療技術短期大学部
2002-02-28
jpn
departmental bulletin paper
http://hdl.handle.net/10091/5255
https://soar-ir.repo.nii.ac.jp/records/6860
0385-1982
AN10402438
紀要
27
57
66
https://soar-ir.repo.nii.ac.jp/record/6860/files/Allied_Med27_06.pdf
application/pdf
592.3 kB
2015-09-25