Skip Navigation



Glycobiology Advance Access published online on May 2, 2008
Glycobiology, doi:10.1093/glycob/cwn035
This Article
Right arrow Advance Access manuscript (PDF) Freely available
Right arrow All Versions of this Article:
18/7/526    most recent
cwn035v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Gil, G.-C.
Right arrow Articles by Cott, K. E. V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gil, G.-C.
Right arrow Articles by Cott, K. E. V.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2008. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Analysis of the N-glycans of Recombinant Human Factor IX Purified from Transgenic Pig Milk

Geun-Cheol Gil1, William H. Velander1,2 and Kevin E. Van Cott1,1

1 Department of Chemical and Biomolecular Engineering, University of Nebraska-Lincoln, Lincoln, NE 68588 USA
2 Progenetics LLC, 1872 Pratt Drive, Suite 1400, Blacksburg, VA 24060 USA

* Corresponding Author: Dr. Kevin Van Cott Phone: 402-472-1743 Fax: 402-472-6989 E-mail: kvancott2{at}unl.edu

Glycosylation of recombinant proteins is of particular importance because it can play significant roles in the clinical properties of the glycoprotein. In this work, the N-glycan structures of recombinant human Factor IX (tg-FIX) produced in the transgenic pig mammary gland were determined. The majority of the N-glycans of tg-FIX are complex, bi-antennary with one or two terminal N-acetylneuraminic acid (Neu5Ac) moieties. We also found that the N-glycan structures of tg-FIX produced in the porcine mammary epithelial cells differed with respect to N-glycans from glycoproteins produced in other porcine tissues. Tg-FIX contains no detectable Neu5Gc, the sialic acid commonly found in porcine glycoproteins produced in other tissues. Additionally, we were unable to detect glycans in tg-FIX that have a terminal Gal{alpha}(1,3)Gal disaccharide sequence, which is strongly antigenic in humans. The N-glycan structures of tg-FIX are also compared to the published N-glycan structures of recombinant human glycoproteins produced in other transgenic animal species. While tg-FIX contains only complex structures, antithrombin III (goat), C1 inhibitor (rabbit), and lactoferrin (cow) have both high mannose and complex structures. Collectively, these data represent a beginning point for the future investigation of species-specific and tissue/cell-specific differences in N-glycan structures among animals used for transgenic animal bioreactors.

Key words: glycoprotein / Factor IX / glycosylation / mammary gland / transgenic animal


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.