Effect of the Multimeric Structure of the Factor Vill/von Willebrand Factor Protein on Binding to Platelets
نویسنده
چکیده
The characteristics of the intact factor VIll/von Willebrand factor protein binding to human platelets was compared to 2-mercaptoethanol-treated factor VIll/von Willebrand factor protein and to fractions of plasma factor VIll/von Willebrand factor protein that elute after the void volume. These studies indicate that the factor VIlI/von Willebrand factor protein larger size oligomers bind preferentially with high affinity to low capacity sites on human platelets. The intermediate and smaller size oligomers bind with intermediate or low affinity to sites with a much greater capacity. The results from binding analysis are also paralleled by the competitive inhibition of the intact factor VIll/von Willebrand factor protein by the various 2-mercaptoethanol-
منابع مشابه
Factor Vill/von Willebrand Factor Binding to von Willebrand’s Disease Platelets
A form of von Willebrand’s disease has been described with enhanced ristocetin-induced platelet aggregation and anodal migration of the factor VIll/von Willebrand factor protein (type lIb). We studied two families with this form of von Willebrand s disease and macrothrombocytopenia. We have found that these platelets bind more of the normal and intermediate-sized multimers of the factor VIll/vo...
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The characteristics of the intact factor VIII/von Willebrand factor protein binding to human platelets was compared to 2-mercaptoethanol-treated factor VIII/von Willebrand factor protein and to fractions of plasma factor VIII/von Willebrand factor protein that elute after the void volume. These studies indicate that the factor VIII/von Willebrand factor protein larger size oligomers bind prefer...
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