Production of Defined Lycosylation Variants of Secreted Human Glycoprotein Therapeutics by Coexpression with Human Recombinant Glycosyl Transferases in BHK-21 Cells View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2002

AUTHORS

P. Schlenke , E. Grabenhorst , J. Costa , M. Nimtz , H. S. Conradt

ABSTRACT

To investigate the stability of a BHK-21 A cell line transfected with human EPO (huEPO) and the human α2,6-sialyltransferase ST6N (huST6N), the cell line was cultivated over a time period of 18 days in a 2.5 L perfused bioreactor in protein- and serum-free medium and under physiological stress after addition of ammonium. The stability of gene expression and the activity of the newly introduced huST6N and the endogenous α2,3-sialyltransferase (α2,3-ST) were analyzed during the different cultivation conditions by RT-PCR and in vitro assays. Furthermore, the purified secreted huEPO was analyzed by western blot and the liberated N-glycans were characterized by HPAEC-PAD analysis. The results confirmed the stability of the cell line with respect to the expression of the newly introduced human proteins even under physiological stress. The elevated ammonium concentration led to reversible changes on the EPO N-glycans. More... »

PAGES

185-190

Book

TITLE

New Developments and New Applications in Animal Cell Technology

ISBN

0-7923-5016-2

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/0-306-46860-3_33

DOI

http://dx.doi.org/10.1007/0-306-46860-3_33

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1019481482


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