Open AccessCharacterization and 400‐MHz 1 H‐NMR analysis of urinary fucosyl glycoasparagines in fucosidosis
Author(s) -
MICHALSKI JeanClaude,
WIERUSZESKI JeanMichel,
ALONSO Catherine,
CACHE Philippe,
MONTREUIL Jean,
STRECKER Gérard
Publication year - 1991
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1991.tb16302.x
Subject(s) - fucose , residue (chemistry) , chemistry , glycan , galactose , nuclear magnetic resonance spectroscopy , asparagine , stereochemistry , biochemistry , sialic acid , amino acid , glycoprotein
Fucosyl glycoasparagines accumulating in the urine of a patient with fucosidosis were isolated using reversephase HPLC. Structural analysis of 25 glycoasparagines was carried out by combination of methylation and 400 MHz 1 H‐NMR spectroscopy analyses. The compounds represent different steps in the incomplete catabolism of N ‐glycosidically linked glycans, as the result of an α‐ l ‐fucosidase deficiency. All of the glycoasparagines possess a fucose residue α‐1,6‐linked to the GlcNAc 1 residue attached to asparagine. Fucose residues on the peripheral branches were linked either α‐1,3 to GlcNAc residues (X determinant) or α‐1,2 to galactose residues (H determinant). The present study allows precise assignments of the NMR parameters for most of the fucosyl linkages occurring in N ‐glycosidically linked glycans of the N ‐acetyllactosamine type.