@article{oai:soar-ir.repo.nii.ac.jp:00006860,
 author = {寺澤,  文子 and 田中,  仁 and 廣田(川戸洞),  雅子 and 石川,  伸介 and 奥村,  伸生},
 journal = {紀要},
 month = {Feb},
 note = {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)},
 pages = {57--66},
 title = {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},
 volume = {27},
 year = {2002}
}