Hills, Anna E. and Patel, A.K. and Boyd, Paul and James, David C. (1999) Control of therapeutic monoclonal antibody glycosylation. In: 16th Meeting of the European-Society-for-Animal-Cell-Technology (ESACT), Apr 25-29, 1999, Lugano, Switzerland. (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)
Protein N-glycosylation is regulated by the availability of nucleotide sugar substrates. Pels Rijcken et al. 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  . 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:||Conference or workshop item (Paper)|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||I.T. Ekpo|
|Date Deposited:||20 Apr 2009 20:17|
|Last Modified:||07 Jul 2014 15:44|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/16849 (The current URI for this page, for reference purposes)|