July 29 - August 3, 2001
2001 Collagen Gordon Research Conference. Colby-Sawyer College, New London, New Hampshire.

Characterization of Hydroxylated Human Recombinant Collagen From Transgenic Systems. Julio Baez, FibroGen.

Transgenic systems (animals and plants) are attractive for human recombinant biologics as manufacturing platform when over 100 kg per year are required. Gelatin used widely in the pharmaceutical industry for capsules, tablets, as vaccine stabilizers and as plasma expanders at 50,000 metric tons per year. FibroGen is to manufacture recombinant gelatin to satisfy pharmaceutical industry's safety, improved functionality, reproducibility, cost, quality concerns. Multi-ton demand and low cost for recombinant gelatin result in the need to use transgenic systems to produce properly processed collagen used for gelatin manufacturing. This presentation describes results from the characterization of collagen produced as a collaborations between FibroGen and Agracetus, a unit of Monsanto, and Pharming for co-expression in transgenic tobacco of mammalian prolyl 4 hydroxylase (P4H) acting on recombinant human collagen III (rhCIII) and collagen I.