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J. Biol. Chem., Vol. 265, Issue 1, 144-150, Jan, 1990
SW Lin, KJ Smith, D Welsch and DW Stafford
Human blood clotting factor IX, and two chimeric molecules of factor IX, in
which the first epidermal growth factor-like domain or both epidermal
growth factor-like domains have been replaced by that of human factor X,
have been expressed in mouse C127 cells. The recombinants have been
purified using a metal ion-dependent monoclonal antibody specific for
residues 1-42 of human factor IX. All recombinant molecules are activated
normally by human factor XIa in the presence of calcium ion. Activation of
the factor IX recombinants by factor VIIa- tissue factor appears to be
normal for the epidermal growth factor-1 exchange but considerably reduced
for the construction containing both epidermal growth factor-like domains
of factor X. The analysis of gamma- carboxyglutamic acid residues reveals
that all of the purified recombinants are almost fully carboxylated. The
extent of aspartic acid hydroxylation at residue 64 is 60% for all
recombinants. The chimeric molecule with both epidermal growth factor-like
domains from factor X has about 4% normal activity in the activated partial
thromboplastin time assay. In contrast, the construct containing the first
epidermal growth factor-like domain of factor X shows essentially normal
clotting activity. Thus, it is unlikely that this domain is involved in a
unique interaction with factor VIII.
Expression and characterization of human factor IX and factor IX-factor X chimeras in mouse C127 cells
Department of Biology, University of North Carolina, Chapel Hill 27514.
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