Investigation of residues in the fibrin(ogen) γ chain involved in tissue plasminogen activator binding and plasminogen activation

In order to characterize tissue plasminogen activator (t-PA) binding to γ-chain residues in fibrinogen, we generated variant fibrinogens substituting alanine for γD316, γD318, γD320, and γK321. We measured thrombin-catalyzed polymerization and found normal polymerization with γK321A, no polymerizati...

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Veröffentlicht in:	Blood coagulation & fibrinolysis 2004-09, Vol.15 (6), p.451-461
Hauptverfasser:	Wilhelm, Susan E, Lounes, Karim C, Lord, Susan T
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Substitution Biological and medical sciences Blood coagulation. Blood cells Fibrinogen - chemistry Fibrinogen - metabolism Fibrinolysin - biosynthesis Fibrinopeptide A - analysis Fibrinopeptide B - analysis Fundamental and applied biological sciences. Psychology Hematologic and hematopoietic diseases Humans Medical sciences Molecular and cellular biology Mutagenesis, Site-Directed Platelet diseases and coagulopathies Protein Binding Protein Interaction Mapping Tissue Plasminogen Activator - metabolism
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