O-linked N-acetylglucosamine is attached to proteins of the nuclear pore. Evidence for cytoplasmic and nucleoplasmic glycoproteins.
JA Hanover, CK Cohen, MC Willingham… - Journal of Biological …, 1987 - ASBMB
Glycoproteins bearing a single N-acetylglucosamine (GlcNAc) residue attached by an O-
glycosidic linkage to the polypeptide chain (Holt, GD, and Hart, GW (1986) J. Biol. Chem.
261, 8049-8057) have been found to be enriched in the nuclear and soluble fractions of rat
liver. Our goal was to determine the localization and membrane topography of proteins
bearing O-linked GlcNAc using galactosyltransferase and wheat germ agglutinin (WGA) as
membrane-impermeant probes. Latency of the enzyme mannose-6-phosphatase was used …
glycosidic linkage to the polypeptide chain (Holt, GD, and Hart, GW (1986) J. Biol. Chem.
261, 8049-8057) have been found to be enriched in the nuclear and soluble fractions of rat
liver. Our goal was to determine the localization and membrane topography of proteins
bearing O-linked GlcNAc using galactosyltransferase and wheat germ agglutinin (WGA) as
membrane-impermeant probes. Latency of the enzyme mannose-6-phosphatase was used …
