Recombinant human fibrinogen

Medved, L., Litvinovich, S., Ugarova, T. P., Matsuka, Y. V., and Ingham, K. (1997). Domain structure and functional activity of the recombinant human fibrinogen gamma-module (gamtrial 48—111). Biochem. 36, 4685—4693. 

Prunkard, D., Cottingham, L, Gamer, L, Bruce, S., Dalrymple, M., Lasser, G., Bishop, P., and Foster, D. (1996). High-level expression of recombinant human fibrinogen in the milk of transgenic mice. Nat. Biotechnol. 14,867-871. 

Matsuka, Y. V., Medved, L. V., Migliorini, M. M., and Ingham, K. C. (1996). Factor XHIa-catalyzed cross-linking of recombinant alpha C fragments of human fibrinogen. Biochem. 35, 5810-5816. 

Glycoproteomics of AFP, Fibrinogen, and Recombinant Human EPO, Based On the Reverse Glycoblotting Protocol"... 

Expression of recombinant proteins in the milk of transgenic animals is gaining popularity due to simple and cost effective production. Over the past several years, the feasibility of this approach has been demonstrated by the production, at mg mb1 levels, of pharmaceutically relevant monomeric proteins such as human al -antitrypsin, human tPA, human protein C and hexameric fibrinogen [166]. However there are limitations of mammary tissue in making the meaningful post-translational modifications, which has been overcome by co expression of key pro cessing enzymes [167]. 

---