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ENZYMATIC GLYCOSYLATION OF N-LINKED GLYCOPROTEIN GLYCANS
Hammel, M. Schneider, R. Berger, E. G. Gygax, D.
Hammel, M.
Schneider, R.
Berger, E. G.
Gygax, D.
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Issue Date
1991
Submitted date
2024-02-28
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Adobe PDF, 1.56 MB
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Abstract
N-linked glycoprotein glycans were modified by combined use of glycosidases and glycosyltransferases. Human milk 81,4 galactosyltransferase andrat liver 02,6 sialyltransferase were immobilized by covalent or affinity binding methods. These immobilized glycosyltransferases were used in a slurry reactor for continuous glycosylation of endoglycosidase H-treated invertase or r-tPA. Theresulting sialylated glycan chains mimicking the structureof outer complex N-glycansconferred extended plasma half-life time compared to galactosylated glycoprotein.
Citation
Protein glycosylation, 215 - 218
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Book chapter
conference paper
conference paper
Language
en
Description
Series/Report no.
GBF monographs ; Volume 15
ISSN
0930-4320
EISSN
ISBN
1560811846
3527283676
3527283676
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Attribution-NonCommercial-ShareAlike 4.0 International