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Identification of a tetrasialylated monofucosylated tetraantennary N ‐linked carbohydrate chain in human platelet glycocalicin
Author(s) -
Korrel Sophia A.M.,
Clemetson Kenneth J.,
van Halbeek Herman,
Kamerling Johannis P.,
Sixma Jan J.,
Vliegenthart Johannes F.G.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80024-3
Subject(s) - chemistry , glycoprotein , carbohydrate , biochemistry , glycosidic bond , glycopeptide , stereochemistry , carbohydrate conformation , glycosylation , platelet membrane glycoprotein , alpha (finance) , glycan , nuclear magnetic resonance spectroscopy , enzyme , antibiotics , medicine , construct validity , nursing , patient satisfaction
Glycocalicin (140 kDa), the main constituent of the glycoprotein Ib α‐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 1 H‐NMR spectroscopy. A novel tetrasialylated monofucosylated tetraantennary chain was identified in the glycoprotein. It could also be deduced that in all structures the α2→6‐linked NeuAc is attached exclusively at the Galβ1→4GlcNAcβ1→2Manα1→3 antenna, whereas the other antennae can be terminated with α2→3‐linked NeuAc. As minor constituents sialylated N ‐linked carbohydrate chains with a terminal Fucα1→2Galβ1→. sequence were detected.