Construction and characterization of stably transfected BHK-21 cells with human-type sialylation characteristic View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1999-07

AUTHORS

Peter Schlenke, Eckart Grabenhorst, Manfred Nimtz, Harald S. Conradt

ABSTRACT

The human Golgi enzyme CMP-NeuAc:Gal(β1–4)GlcNAc-R α2,6-sialyltransferase (ST6N) was stably coexpressed with human erythropoietin (EPO) from a BHK-21A cell line. The cell line was characterized with respect to the expression and in vitro activity of the ST6N and the endogenous α2,3-sialyltransferase. Detailed structural analysis of the N-linked carbohydrates of the rhuEPO expressed from the new cell line was performed by HPAE-PAD-mapping, MALDI/TOF-MS and methylation analysis after purification of the recombinant protein by immunoaffinity chromatography. This is the first report describing that the human α2,6-sialyltransferase is capable of sialylating, apart from Gal(β1–4)GlcNAc-R, also GalNAc(β1–4)GlcNAc-R motifs in vivo, which is not the case for the endogenous BHK-cell α2,3-sialyltransferase. More... »

PAGES

17-25

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/a:1008049603947

DOI

http://dx.doi.org/10.1023/a:1008049603947

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1041160830

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/19003352


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