Abstract
Recombinant DNA technology has permitted the production of synthetic proteins which are potentially free of human infectious agents. Despite production in foreign cells, these proteins are structurally and functionally comparable to the native proteins. Recombinant clotting factors VIII, IX, VIIa, and von Willebrand factor have the same primary sequence as their plasma counterparts. The secondary and tertiary structures are similar, Post-translational modifications, including proteolytic processing, disulfide bonding, addition and processing of N- and O-linked glycans, γ-carboxylation of glutamic acid residues, β-hydroxylation of aspartic acid residues, sulfation of tyrosine residues, and phosphorylation of serine residues, are similar but not always identical, In some instances. these differences may cause significant functional differences. For example, reduced tyrosine sulfation and serine phosphorylation of recombinant factor IX have been correlated with reduced recovery following intravenous infusion. The specific clotting activity of the recombinant factors, an indication of their coagulant function, is equivalent to that of the plasma factors. Finally, these proteins have been used clinically and shown to correct clinical deficiencies of these proteins in a manner that is similar to replacement with plasma factors. All in all, the promise of recombinant DNA technology for coagulation and other disorders remains bright.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.