Identification of a tetrasialylated monofucosylated tetraantennary N-linked carbohydrate chain in human platelet glycocalicin
Publication date
1988
Authors
Vliegenthart, J.F.G.
Korrel, S.A.M.
Clemetson, K.J.
Halbeek, H. van
Kamerling, J.P.
Sixma, J.J.
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Abstract
Glycocalicin (140 kDa), the main constituent of the glycoprotein Ib alpha-chain (150 kDa) of the human platelet membrane, contains 4 putative N-glycosylation sites. For the structural analysis of the N-glycosidic carbohydrate chains of glycocalicin, the glycoprotein has been subjected to the hydrazinolysis procedure. The acidic carbohydrate chains obtained were fractionated by ion-exchange chromatography on DEAE-Sephadex A-25, subsequently analysed by sugar analysis, anion-exchange chromatography on Mono Q HR 5/5 500 MHz 1H-NMR spectroscopy. A novel tetrasialylated monofucosylated tetraantennary chain was identified in the glycoprotein. It could also be deduced that in all structures the alpha2¨6-linked NeuAc is attached exclusively at the Gal beta 1¨4GlcNAc beta 1¨2Man alpha 1¨3 antenna, whereas the other antennae can be terminated with alpha2¨3-linked NeuAc. As minor constituents sialylated N-linked carbohydrate chains with a terminal Fuc alpha1¨2Gal beta1¨. sequence were detected.