Glycosylation Patterns of a rec-Fusion Protein Expressed in BHK Cells at Different Metabolic States View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2000

AUTHORS

H.J. Cruz , H.S. Conradt , C.M. Peixoto , P.M. Alves , M. Nimtz , E.M. Dias , H. Santos , J.L. Moreira , M.J.T. Carrondo

ABSTRACT

BHK-21 cells expressing a rhIgG-IL2 fusion protein were grown under different nutrient conditions in a continuoussystem. At very low glucose (<0.5 mM) or glutamine (<02 mM) concentrations, a shift towards an energetically more efficient metabolism was observed. Cell specific productivity was maintained under metabolically shifted growth conditions and at the same time a constant energy state was observed. No significant differences in the oligosaccharide structures were observed from the rhIgG-IL2 obtained under the different metabolic states. Only neutral diantennary oligosaccharides with or without core α1-6-linked fucose were detected that carried no, one or two Galβ1-4 linked galactose. The data obtained point to the presence of the classical NeuAcα2-3Galβ1-3GalNAc structure for O-linked oligosaccharides that are present in the IL-2 moiety of the protein. More... »

PAGES

241-243

Book

TITLE

Animal Cell Technology: Products from Cells, Cells as Products

ISBN

978-0-7923-6075-9
978-0-306-46875-9

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/0-306-46875-1_55

DOI

http://dx.doi.org/10.1007/0-306-46875-1_55

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1011729005


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