Characterization of an abnormal fibrinogen Osaka V with the replacement of gamma-arginine 375 by glycine. The lack of high affinity calcium binding to D-domains and the lack of protective effect of calcium on fibrinolysis.-Reference-Cited by-同舟云学术

Characterization of an abnormal fibrinogen Osaka V with the replacement of gamma-arginine 375 by glycine. The lack of high affinity calcium binding to D-domains and the lack of protective effect of calcium on fibrinolysis.

Published:1992-02 Issue:4 Volume:267 Page:2753-2759
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Yoshida N,Hirata H,Morigami Y,Imaoka S,Matsuda M,Yamazumi K,Asakura S

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference70 articles.

1. Variants of Human Fibrinogen;Rupp,1984

2. Fibrinogen houston: A dysfibrinogen exhibiting defective fibrin monomer aggregation and α-chain cross-linkages

3. Fibrinogen Chapel Hill II: Defective in reactions with thrombin, factor XIIIa and plasmin

4. Fibrinogen;Rupp,1982

5. A new type of congenital dysfibrinogenaemia with defective fibrin lysis—Dusard syndrome: possible relation to thrombosis

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