ABSTRACT
This chapter argues that the therapeutic Recombinant activated coagulation factor VII (rFVIIa) molecule exerts its function, factor VIIa (FVIIa) has low biological activity and poor membrane affinity. The procoagulant and antifibrinolytic effects of high-dose rFVIIa promote both clot formation and clot stability in the absence of a functional Xase complex. The structural characterization of rFVIIa includes determination of the amino acid sequence as well as determination of the posttranslational modifications. Human FVIIa contains two potential N-linked glycosylation sites at N145 in the light chain and at N322 in the heavy chain, and both sites are found to be fully occupied in rFVIIa. Based on the determination of the carbohydrate composition of pdF-VIIa and rFVIIa, the N-linked glycosylation of the two FVIIa forms is similar, the most pronounced difference being a higher fucose content and a lower sialic acid content of rFVIIa compared with pdFVIIa.
