Abstract
O-linked GlcNAc β-linked to Ser/Thr, where GlcNAc remains unsubstituted, is found in a number of cytoplasmic, nuclear and nuclear envelope proteins in pecies from yeast to man, including transcription factors, crystallins, kinases and viral glycoproteins. These O-GlcNAc residues have been detected by using O-GlcNAc containing glycoproteins as a substrate for bovine milk β4-Gal-transferase with subsequent release of Galβ1-4G1cNAc-OH by beta-elimination. The functions of O-G1cNAc have been suggested to be assembly and maintenance of protein complexes, regulation of protein synthesis and control of protein phosphorylation.1
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© 1997 Springer-Verlag Berlin Heidelberg
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Brockhausen, I., Kuhns, W. (1997). Less Common O-Linked Carbohydrates of Glycoproteins. In: Glycoproteins and Human Disease. Medical Intelligence Unit. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-21960-7_7
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DOI: https://doi.org/10.1007/978-3-662-21960-7_7
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