Control of therapeutic monoclonal antibody glycosylation

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
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:	16 Nov 2021 09:54 UTC
Resource URI:	https://kar.kent.ac.uk/id/eprint/16849 (The current URI for this page, for reference purposes)

University of Kent Author Information

James, David C..

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