Modification of cell surfaces by enzymatic introduction of special sialic acid analogues

Taking advantage of the defined acceptor specifity of rat liver α2,6-sialyltransferase, N-linked Ga1β1,4GlcNAc-sequences of glycoconjugates at the plasma membrane of viable human erythrorytes and lymphoblastic IN-9 cells were modified to terminate in three NeuAc analogues endowed with special bemche...

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Main Authors: Kosa, Renate E. (Author) , Brossmer, Reinhard (Author) , Groß, Hans Jürgen (Author)
Format: Article (Journal)
Language:English
Published: 15 February 1993
In: Biochemical and biophysical research communications
Year: 1993, Volume: 190, Issue: 3, Pages: 914-920
ISSN:1090-2104
DOI:10.1006/bbrc.1993.1136
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1006/bbrc.1993.1136
Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S0006291X83711368
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Author Notes:Renate E. Kosa, Reinhard Brossmer, Hans Jürgen Groß
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Summary:Taking advantage of the defined acceptor specifity of rat liver α2,6-sialyltransferase, N-linked Ga1β1,4GlcNAc-sequences of glycoconjugates at the plasma membrane of viable human erythrorytes and lymphoblastic IN-9 cells were modified to terminate in three NeuAc analogues endowed with special bemchemical properties: sialidase-resistant 9-amino-NeuAc, O-acetylesterase-resistant 9-acetamido-NeuAc and photolabile 9-azido-NeuAc. Incorporation of the latter analogues and of parent NeuAc proceeded to similar values, whereas 9-amino-NeuAc yielded slightly reduced values.
Item Description:Elektronische Reproduktion der Druck-Ausgabe 25. Mai 2002
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Physical Description:Online Resource
ISSN:1090-2104
DOI:10.1006/bbrc.1993.1136