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QUARTERLY The participation of ribosome–UDP-GalNAc complex in the initiation of protein glycosylation in vitro

By Anna Paszkiewicz-gadek, Halina Porowska and Andrzej Gindzieñski

Abstract

The gastric epithelial cells ribosome–UDP-GalNAc complex is a donor of UDP-GalNAc as the substrate for N-acetylgalactosaminyltransferase, which catalyse the transfer of GalNAc residue to the polypeptide, existing on polysomes. It was observed that the deglycosylated porcine mucin and synthetic peptide (PTSSPIST) can be also glycosylated with participation of N-acetylgalactosaminyltransferase and ribosome– UDP-GalNAc complex. The probability of the ribosome–UDP-GalNAc complex as an intermediate in the O-glycosylation is considered. Glycoprotein biosynthesis, especially its sequential O-glycosylation, has been a matter of investigations for many years. In contrast to N-glycosylation, O-glycosylation does not begin with the transfer of oligosaccharide from a dolichol precursor, but with the addition of a single monosaccharide from the nucleotide substrate to acceptors. In the case of mucintyp

Year: 2013
OAI identifier: oai:CiteSeerX.psu:10.1.1.321.9498
Provided by: CiteSeerX
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