Site-directed mutagenesis of a soluble recombinant fragment of platelet glycoprotein Ib alpha demonstrating negatively charged residues involved in von Willebrand …
We have expressed in mammalian cells a fragment (residues 1-302) of the alpha chain of
platelet glycoprotein (GP) Ib containing the von Willebrand factor-(vWF) binding site. The
secreted soluble protein had an apparent molecular mass of 45 kDa and reacted with
conformation-dependent monoclonal antibodies that bind only to native GP Ib, thus
demonstrating its proper folding. After insolubilization on nitrocellulose membrane, the
recombinant GP Ib alpha fragment bound soluble vWF in the presence of ristocetin or …
platelet glycoprotein (GP) Ib containing the von Willebrand factor-(vWF) binding site. The
secreted soluble protein had an apparent molecular mass of 45 kDa and reacted with
conformation-dependent monoclonal antibodies that bind only to native GP Ib, thus
demonstrating its proper folding. After insolubilization on nitrocellulose membrane, the
recombinant GP Ib alpha fragment bound soluble vWF in the presence of ristocetin or …
