B:b interactions are essential for polymerization of variant fibrinogens with impaired holes 'a'

Fibrin polymerization is mediated by interactions between knobs 'A' and 'B' exposed by thrombin cleavage, and holes 'a' and 'b' always present in fibrinogen. The role of A:a interactions is well established, but the roles of knob:hole interactions A:b, B:b or...

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Veröffentlicht in:	Journal of thrombosis and haemostasis 2007-12, Vol.5 (12), p.2352-2359
Hauptverfasser:	Okumura, N, Terasawa, F, Haneishi, A, Fujihara, N, Hirota-Kawadobora, M, Yamauchi, K, Ota, H, Lord, S T
Format:	Artikel
Sprache:	eng
Schlagworte:	Batroxobin - metabolism Binding Sites Binding, Competitive Chromatography, High Pressure Liquid Electrophoresis, Polyacrylamide Gel Factor XIIIa - metabolism Fibrinogen - chemistry Fibrinogen - genetics Fibrinogen - metabolism Fibrinopeptide A - chemistry Fibrinopeptide A - metabolism Fibrinopeptide B - chemistry Fibrinopeptide B - metabolism Kinetics Microscopy, Electron, Scanning Models, Biological Mutation Nephelometry and Turbidimetry Oligopeptides - metabolism Protein Binding Protein Conformation Protein Structure, Tertiary Thrombin - metabolism
Online-Zugang:	Volltext
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