Hills, Anna E. and Patel, A.K. and Boyd, Paul and James, David C. (1999) Control of therapeutic monoclonal antibody glycosylation. In: Bernard, Alain and Griffiths, Bryan and Noe, W. and Wurm, Florian, eds. Animal Cell Technology: Products from Cells, Cells as Products Proceedings of the 16th ESACT Meeting. Springer, Dordrecht, Netherlands, pp. 255-257. ISBN 978-0-7923-6075-9. E-ISBN 978-0-306-46875-9. (doi:10.1007/0-306-46875-1_58) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:16849)
The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. | |
Official URL: http://dx.doi.org/10.1007/0-306-46875-1_58 |
Abstract
Protein N-glycosylation is regulated by the availability of nucleotide sugar substrates. Pels Rijcken et al.[3] have proposed that elevated cytosolic levels of UDP-N-acetylhexosamine impaired the transport of CMPNeuAc into the Golgi, which lead to decreased sialylation. Addition of glucosamine to cell culture medium has resulted in an increase in antennarity of N-glycans [4] . By manipulating the levels of nucleotide sugar precursors available to NS0 cells (by additions to the cell culture medium) a strategy for controlling product glycosylation could be devised.
Item Type: | Book section |
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DOI/Identification number: | 10.1007/0-306-46875-1_58 |
Uncontrolled keywords: | Cell Culture Medium; Chinese Hamster Ovary Cell; High Performance Liquid Chromatographic Method; Amino Acid Deprivation; Biotechnology Analytical |
Subjects: | Q Science |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | I.T. Ekpo |
Date Deposited: | 20 Apr 2009 20:17 UTC |
Last Modified: | 05 Nov 2024 09:52 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/16849 (The current URI for this page, for reference purposes) |
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