Effects of Ammonia and Glucosamine on the Glycsosylation Pattern of Recombinant Proteins Expressed from BHK-21 Cells View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1995

AUTHORS

M. Gawlitzek , U. Valley , M. Nimtz , R. Wagner , H. S. Conradt

ABSTRACT

In order to analyze the effect of different culture conditions on the N-glycosylation of polypeptides, a recombinant hu-IL-2 variant protein (IL-Mu6) expressed from BHK-21 cells has been used as a model. This model protein bears an artificial N-glycosylation recognition site (Asn-Xxx-Ser/Thr) generated by a single amino acid substitution (Glu100 → Asn). The effects of ammonia and glucosamine on the N-glycosylation of this recombinant protein were examined using perfused 2-liter double-membrane stirrer bioreactors under defined culture conditions. Products from the various cell culture supernatants were characterized by western blotting, peptide mapping, amino acid sequence analysis as well as by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAEC-PAD), methylation analysis and matrix-assisted laser-desorption ionization mass spectrometry (MALDI-MS). All oligosaccharides were found to be of the complex-type, with major differences in the sialylation-state, the degree of proximal fucosylation and the antennarity. More... »

PAGES

379-384

References to SciGraph publications

Book

TITLE

Animal Cell Technology: Developments Towards the 21st Century

ISBN

978-94-010-4195-9
978-94-011-0437-1

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-94-011-0437-1_60

DOI

http://dx.doi.org/10.1007/978-94-011-0437-1_60

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1005773080


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