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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.

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References and Acknowledgements

  1. Heal, R., McGivan, J. (1998) Induction of calreticulin expression in response to amino acid deprivation in Chinese Hamster Ovary cells. Biochem.J.329 389–394.

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A. Bernard B. Griffiths W. Noé F. Wurm

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© 1999 Kluwer Academic Publishers

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Hills, A., Patel, A., Boyd, P., James, D. (1999). Control of Therapeutic Monoclonal Antibody Glycosylation. In: Bernard, A., Griffiths, B., Noé, W., Wurm, F. (eds) Animal Cell Technology: Products from Cells, Cells as Products. Springer, Dordrecht. https://doi.org/10.1007/0-306-46875-1_58

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  • DOI: https://doi.org/10.1007/0-306-46875-1_58

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-0-7923-6075-9

  • Online ISBN: 978-0-306-46875-9

  • eBook Packages: Springer Book Archive

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