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Matrix‐assisted laser desorption/ionization mass spectrometry of carbohydrates
Author(s) -
Harvey David J.
Publication year - 1999
Publication title -
mass spectrometry reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 126
eISSN - 1098-2787
pISSN - 0277-7037
DOI - 10.1002/(sici)1098-2787(1999)18:6<349::aid-mas1>3.0.co;2-h
Subject(s) - chemistry , exoglycosidase , mass spectrometry , chromatography , matrix assisted laser desorption/ionization , fragmentation (computing) , sample preparation , analytical chemistry (journal) , glycan , mass spectrum , protein mass spectrometry , desorption , tandem mass spectrometry , glycoprotein , biochemistry , organic chemistry , adsorption , computer science , operating system
This review describes the application of matrix‐assisted laser desorption/ionization (MALDI) mass spectrometry to carbohydrate analysis and covers the period 1991–1998. The technique is particularly valuable for carbohydrates because it enables underivatised, as well as derivatised compounds to be examined. The various MALDI matrices that have been used for carbohydrate analysis are described, and the use of derivatization for improving mass spectral detection limits is also discussed. Methods for sample preparation and for extracting carbohydrates from biological media prior to mass spectrometric analysis are compared with emphasis on highly sensitive mass spectrometric methods. Quantitative aspects of MALDI are covered with respect to the relationship between signal strength and both mass and compound structure. The value of mass measurements by MALDI to provide a carbohydrate composition is stressed, together with the ability of the technique to provide fragmentation spectra. The use of in‐source and post‐source decay and collision‐induced fragmentation in this context is described with emphasis on ions that provide information on the linkage and branching patterns of carbohydrates. The use of MALDI mass spectrometry, linked with exoglycosidase sequencing, is described for N‐linked glycans derived from glycoproteins, and methods for the analysis of O‐linked glycans are also covered. The review ends with a description of various applications of the technique to carbohydrates found as constituents of glycoproteins, bacterial glycolipids, sphingolipids, and glycolipid anchors. © 1999 John Wiley & Sons, Inc., Mass Spec Rev 18: 349–451, 1999