This work demonstrates that (N-acetyl[14C]glucosamine)2 is transferred from dolichyl pyrophosphate-(N-acetyl[14C]glucosamine)2 to endogenous nuclear glycoproteins. The (N-acetyl[14C]glucosamine)2 moiety is N-linked, since it can be released from the tryptic glycopeptides by N-glycosidase F and by hydrazinolysis, but not by beta-elimination. The biological significance of this direct transfer of N,N'-diacetylchitobiose to nuclear proteins remains to be elucidated.
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Effect of GTP on the dolichol pathway for protein glycosylation in rat liver microsomes.
Biochem J
December 1993
Laboratory of Biological Chemistry, Katholieke Universiteit Leuven, Belgium.
Incubation of native rat liver microsomes with GTP resulted in enhanced incorporation of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc into lipid acceptors. The stimulation of GlcNAc transfer by GTP was specific for GTP; ATP exerted no effect. The GTP effect was blocked by a non-hydrolysable GTP analogue guanosine 5'-[beta gamma-imido]triphosphate, indicating that GTP hydrolysis was crucial.
View Article and Find Full Text PDFHuman erythrocyte membranes contain the enzymes responsible for the synthesis of dolichol-P-glucose, dolichol-P-mannose, dolichol-PP-N-acetylglucosamine, dolichol-PP-NN' diacetylchitobiose and of dolichol-PP-oligosaccharides containing NN' diacetylchitobiose and mannose or the same sugar residues plus glucose. The transfer of the oligosaccharide moieties from the dolichol-PP-oligosaccharides to endogenous proteins could not be detected. These enzymes appeared to be integral membrane proteins.
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