Open AccessStructure of the N‐Linked Oligosaccharides from Tridacnin, a Lectin Found in the Haemolymph of the Giant Clam Hippopus Hippopus
Author(s) -
Puanglarp Narongsak,
Oxley David,
Currie Graeme J.,
Bacic Antony,
Craik David J.,
Yellowlees David
Publication year - 1995
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1995.0873a.x
Subject(s) - glycan , lectin , chemistry , residue (chemistry) , asparagine , glycoprotein , biochemistry , hemolymph , glycopeptide , oligosaccharide , mass spectrometry , mannose , electrospray ionization , stereochemistry , peptide , chromatography , amino acid , antibiotics
Tridacnin, 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‐ N 4 ‐( N ‐acetyl‐β‐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, 1 H‐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.