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  • Title: The role of the epidermal growth factor-1 and hydrophobic stack domains of human factor IX in binding to endothelial cells.
    Author: Cheung WF, Straight DL, Smith KJ, Lin SW, Roberts HR, Stafford DW.
    Journal: J Biol Chem; 1991 May 15; 266(14):8797-800. PubMed ID: 1851159.
    Abstract:
    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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