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Primary structure of the propeptide and factor VIII-binding domain of bovine von Willebrand factor
1Unité de Recherches sur l'Hémostase et la Thrombose, INSERM U 143, Hôpital de Bicêtre, France.
Biochimica Et Biophysica Acta
|April 25, 1997
Abstract:
A 2811 base-pair cDNA, encoding the amino-terminal part of the bovine pre-pro-von Willebrand factor, was characterized and sequenced. The deduced amino acid sequence shares significant homology with the human von Willebrand antigen II and the amino-terminal part of the factor VIII-binding domain of von Willebrand factor. In contrast to human, there is no RGD motif in the bovine von Willebrand antigen II. High levels of Cys, characteristic of D domains, are also found in bovine and the Cys position is markedly conserved between the two species.