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pubmed-article:7588729pubmed:abstractTextTridacnin, a glycoprotein lectin, was isolated from the symbiotic marine clam Hippopus hippopus and the structure of its major N-glycan chains determined. Tridacnin contains only N-linked glycans which were quantitatively cleaved by peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F. Following purification by anion-exchange HPLC, the structures of the oligosaccharides were established using a combination of electrospray ionisation mass spectrometry, 1H-NMR spectroscopy and linkage analysis. The N-glycans are primarily of the oligomannose type but, in addition, some contain a novel 6-O-Me group on the terminal mannose residue of the chain. The N-glycan chains had the following structures. [formula: see text]lld:pubmed
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pubmed-article:7588729pubmed:pagination873-80lld:pubmed
pubmed-article:7588729pubmed:dateRevised2007-7-23lld:pubmed
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pubmed-article:7588729pubmed:articleTitleStructure of the N-linked oligosaccharides from tridacnin, a lectin found in the haemolymph of the giant clam Hippopus hippopus.lld:pubmed
pubmed-article:7588729pubmed:affiliationDepartment of Molecular Sciences, James Cook University, Townsville, Queensland, Australia.lld:pubmed
pubmed-article:7588729pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:7588729pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed