Human coagulation factor VII (FVIIa). FVIIa is a serine protease of 406 residues. The active two-chain enzyme is generated by specific cleavage after R152 . Posttranslational modifications of the FVII molecule include: (i) y-carboxylation of ten glutamic acid residues in the N-terminal part of the molecule; (ii) N-glycosylation of asparagine residues in positions 145 and 322; and (iii) O-glycosylation of S52 and S60. y : y-carboxyglutamic acid; *: glycosylation sites; activation site; O: catalytic site residues.
alkylation of the disulfide bridges, the light and heavy chains were separated. Each of the two chains was subjected to peptide mapping by tryptic digestion and reverse-phase high performance liquid chromatography (HPLC), and the peptide fragments were characterized by N-terminal sequence analysis. The amino acid sequence determined for rFVIIa (Figure 10.3) was identical to the amino acid sequence of pdFVIIa, and in accordance with the sequence deduced from complementary deoxyribonucleic acid (cDNA) .
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