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J. Biol. Chem., Vol. 266, Issue 14, 8797-8800, 05, 1991

The role of the epidermal growth factor-1 and hydrophobic stack domains of human factor IX in binding to endothelial cells

WF Cheung, DL Straight, KJ Smith, SW Lin, HR Roberts and DW Stafford
Department of Biology, University of North Carolina, Chapel Hill 27599.

To determine the function and specificity in factor IX of the first epidermal growth factor (EGF)-like domain and the eight-amino acid hydrophobic stack encoded by exon C (residues 39-46), these domains were replaced by the corresponding polypeptide regions of factor X and chimeric proteins were produced in human embryo kidney cells. Both chimeras were activated by factor XIa at a rate similar to plasma factor IX and exhibited calcium-dependent fluorescence quenching similar to plasma factor IX. Both chimeras competed equally for binding to the endothelial cell receptor. Our findings make it unlikely that the first EGF-like domain or the hydrophobic stack of factor IX are responsible for the specific binding of factor IX to its endothelial cell receptor.
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