Premium
Tandem mass spectrometry for the characterisation of sulphated‐phosphorylated analogues of the carbohydrate–protein linkage region of proteoglycans
Author(s) -
Antonopoulos Aristotelis,
Favetta Patrick,
Jacquinet JeanClaude,
Lafosse Michel
Publication year - 2005
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.941
Subject(s) - chemistry , glycosidic bond , tandem mass spectrometry , oligosaccharide , phosphate , phosphorylation , mass spectrometry , carbohydrate , fast atom bombardment , carboxylate , stereochemistry , molecule , biosynthesis , biochemistry , chromatography , organic chemistry , enzyme
Carbohydrate–protein linkage region of proteoglycans is a key oligosaccharide structure because their sulphated and/or phosphorylated analogues control the biosynthesis of gluco saminoglycans or galacto saminoglycans. Therefore, synthesised sulphated and/or phosphorylated analogues were characterised by tandem mass spectrometry in the negative‐ion mode. Results demonstrated that the product ion profile was characterised by glycosidic and cross‐ring cleavages depending on the position and the type of the charged group (sulphate, phosphate or carboxylate). When the above compounds were sulphated and phosphorylated, the ion found at m / z 79 was the only one that demonstrated a phosphate group on the structure. The data also suggested that when a sodium cation was present in a sulphated and phosphorylated structure, the phosphate group in most cases was neutralised by the sodium cation, and therefore cleaved off the molecule, while the sulphate group was carrying the negative charge. Copyright © 2005 John Wiley & Sons, Ltd.