Glycomics on pig derived human glycoproteins

ISBN-13: 9783639170283 / Angielski / Miękka / 2009 / 256 str.

Geun-Cheol Gil

Opis

Glycosylation of recombinant proteins is of particular importance because it can play significant roles in the clinical properties of the glycoprotein, such as enzyme activity, protein stability, pharmacokinetics, and immunogenicity. In this work, the N-glycan structures of recombinant human Factor IX (tg-FIX) and Protein C (tg-PC) produced in the transgenic pig mammary gland were determined. It has been found that the majority of N-glycans of tg-FIX and tg-PC are complex bi- and tri-antennary with one or two terminal N-acetylneuraminic acid moieties. There were significant species-specific and tissue/cell-specific differences in N-glycan structures among animals used for transgenic animal bioreactors. N-glycan profiles of tg-FIX were consistent during lactation with respect to the overall distribution of sialylated vs. neutral oligosaccharides. The results show that the porcine mammary gland can be a viable candidate bioreactor for production of recombinant human glycoproteins that require complex, sialylated N-linked glycans.

O autorze

Dr. Gil recieved Ph.D. in the field of Glycomics and
Glycoproteomics at the University of Nebraska, Lincoln, NE, USA
in 2006. Now, he continues to work on Glycomics research at
Sandia National Laboratories, Livermore, CA, USA.