The formation of β fibrin requires a functional a site

Annals of the New York Academy of Sciences

Volumn 936, Issue , 2001, Pages 219-222

  Hogan, Kelly A ^a   Bolliger, Bettina ^a   Okumura, Nobuo ^b   Lord, Susan T ^a  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^b SHINSHU UNIVERSITY   (Japan)

Author keywords

Polymerization sites; fibrin

Indexed keywords

FIBRIN DERIVATIVE; FIBRINOGEN; RECOMBINANT PROTEIN;

BLOOD CLOTTING; CONFERENCE PAPER; FIBRIN FORMATION; FIBRIN POLYMERIZATION; PROTEIN INTERACTION;

EID: 0034964448     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2001.tb03509.x     Document Type: Conference Paper

References (7)

1. Studies on a procoagulant fraction of southern copperhead snake venom: The preferential release of fibrinopeptide B
2. Fibrinopeptide B and aggregation of fibrinogen
3. Studies on the ultrastructure of fibrin lacking fibrinopeptide B (β-fibrin)
4. Conformational changes in fragments D and double D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-Amide
5. Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides
6. Recombinant fibrinogen Vlissingen/Frankfurt IV. The deletion of residues 319 and 320 from the γ-chain of fibrinogen alters calcium binding, fibrin polymerization, cross-linking, and platelet aggregation
7. Severely impaired polymerization of recombinant fibrinogen γ-364 Asp→His, the substitution discovered in a heterozygous individual