Intrinsic stability and functional properties of disulfide bond‐stabilized coagulation factor VIIIa variants

Background: The utility of purified coagulation factor (F)VIII for treatment of hemophilia A is limited in part by its instability following activation by thrombin, which is caused by spontaneous dissociation of the A2 domain from the activated FVIII (FVIIIa) heterotrimer. To prevent this A2 domain...

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Veröffentlicht in:	Journal of thrombosis and haemostasis 2006-06, Vol.4 (6), p.1315-1322
Hauptverfasser:	GALE, A. J., RADTKE, K.‐P., CUNNINGHAM, M. A., CHAMBERLAIN, D., PELLEQUER, J.‐L., GRIFFIN, J. H.
Format:	Artikel
Sprache:	eng
Schlagworte:	Biochemistry, Molecular Biology disulfide bond Factor IXa Factor IXa - metabolism Factor VIII Factor VIII - chemistry Factor VIII - metabolism Factor VIII - therapeutic use Factor VIIIa Factor VIIIa - chemistry Factor VIIIa - genetics Factor VIIIa - metabolism Factor VIIIa - therapeutic use Hemophilia A Hemophilia A - drug therapy Life Sciences Mutation Protein Binding Protein C Protein C - metabolism Protein Conformation Protein Denaturation Protein Engineering Recombinant Proteins Recombinant Proteins - chemistry Recombinant Proteins - metabolism Recombinant Proteins - therapeutic use Structural Biology Surface Plasmon Resonance Thrombin Thrombin - metabolism von Willebrand Factor von Willebrand Factor - metabolism
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