What is the difference between recombinant Factor VIIa and purified derived Factor Factor VIIa?
  Based on high performance liquid chromatography, amino acid analysis, peptide mapping, and Edman degradation, the protein backbone of recombinant Factor VIIa was found to be identical with human purified Factor VIIa. Gamma-carboxylation of the two factors was shown to be nearly identical. The 10 glutamic acid residues in the Gla domain are fully gamma-carboxylated in the purified Factor VIIa, whereas in recombinant Factor VIIa, nine residues are fully and one residue is partially gamma-carboxylated in the corresponding positions. Despite minor differences in the sialic acid and fucose contents, the overall carbohydrate compositions were nearly identical in recombinant Factor VIIa. Furthermore, the enzymatic properties of recombinant Factor VIIa have been evaluated and have been shown to be identical to those of purified Factor VIIa.
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