| Literature DB >> 16664336 |
Abstract
The transport and accumulation of phytohemagglutinin in developing bean (Phaseolus vulgaris L.) cotyledons is accompanied by the transient presence of N-acetylglucosamine (GlcNAc) residues on the oligosaccharide sidechains of this glycoprotein. These peripheral GlcNAc residues can be distinguished from those in the chitobiose portion of the oligosaccharide sidechains by their sensitivity to removal by the exoglycosidase beta-N-acetylglucosaminidase. GlcNAc residues sensitive to removal by beta-N-acetylglucosaminidase are present not only on phytohemagglutinin, but also on other newly synthesized proteins. The enzyme UDPGlcNAc:glycoprotein GlcNAc-transferase which transfers GlcNAc residues to glycoproteins was first described by Davies and Delmer (Plant Physiol 1981 68: 284-291). The data presented here show that this enzyme is associated with the Golgi complex of developing cotyledons.Entities:
Year: 1985 PMID: 16664336 PMCID: PMC1064833 DOI: 10.1104/pp.78.4.835
Source DB: PubMed Journal: Plant Physiol ISSN: 0032-0889 Impact factor: 8.340