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• W2077515296 abstract "This report describes the structural details of a unique N-linked valence epitope on the major protein within the extrapallial (EP) fluid of the mollusk, Mytilus edulis. Fluids from this area are considered to be responsible for shell expansion by a self-assembly process that provides an organic framework for the growth of CaCO3 crystals. Previous reports from our laboratories have described the purification and amino acid sequence of this EP protein, which was found to be a glycoprotein (EPG) of approximately 28 KDa with 14.3% carbohydrate on a single N-linked consensus site. Described herein is the de novo sequence of the major glycan and its glycomers. The sequence was determined by ion trap sequential mass spectrometry (ITMSn) resolving structure by tracking precursor-product relationships through successive rounds of collision induced disassociation (CID), thereby spatially resolving linkage and branching details within the confines of the ion trap. Three major glycomers were detected, each possessing a 6-linked fucosylated N-linked core. Two glycans possessed four and five identical antennae, while the third possessed four antennas, but with an additional methylfucose 2-linked to the glucuronic acid moiety, forming a pentasaccharide. The tetrasaccharide structure was: 4-O-methyl-GlcA(1–4)[GlcNAc(1–3)]Fuc(1–4)GlcNAc, while the pentasaccharide was shown to be as follows: mono-O-methyl-Fuc(1–2)-4-O-methyl-GlcA(1–4)[GlcNAc(1–3)]Fuc(1–4)GlcNAc. Samples were differentially deuteriomethylated (CD3/CH3) to localize indigenous methylation, further analyzed by high resolution mass spectrometry (HRMS) to confirm monomer compositions, and finally gas chromatography mass spectrometry (GC–MS) to assign structural and stereoisomers. The interfacial shell surface location of this major extrapallial glycoprotein, its calcium and heavy metal binding properties and unique structure suggests a probable role in shell formation and possibly metal ion detoxification. A closely related terminal tetrasaccharide structure has been reported in spermatozoan glycolipids of freshwater bivalves." @default.
• W2077515296 created "2016-06-24" @default.
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• W2077515296 date "2013-09-17" @default.
• W2077515296 modified "2023-10-18" @default.
• W2077515296 title "Anomalous <i>N</i>-Glycan Structures with an Internal Fucose Branched to GlcA and GlcN Residues Isolated from a Mollusk Shell-Forming Fluid" @default.
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• W2077515296 doi "https://doi.org/10.1021/pr4006734" @default.
• W2077515296 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3792654" @default.
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