This doctoral thesis aimed at combining liquid chromatography and mass spectrometry for the analysis of protein-linked carbohydrates. To this end, I first evaluated the potential of labels for oligosaccharides for chromatographic and mass spectrometric applications. Fluorescence characteristics and ionization properties in matrix-assisted laser desorption and electrospray ionization varied only within a narrow range. The advantage of labeled over free glycans for mass spectrometric detection was marginal. In the course of this study, I came across a very simple post-labeling purification method applicable to N- and O-glycans. Since advantages gained from labeling of glycans are rather small, I focused on free, borohydride reduced glycans and porous graphitic carbon chromatography coupled on-line to ESI-MS. During this work, the deleterious effect of voltage-induced electrosorption for acidic glycans was described. Further, the influence of eluent pH and ionic strength on chromatographic behavior was investigated and the relative detection intensities of neutral and charged glycans in negative and positive ionization mode were determined. Finally, sample clean-up and column regeneration procedures led to a highly reproducible online LC-ESI-MS approach, suitable for low fmol amounts of glycans. Isomers, differing in the linkage of sialic acid and galactose, could be easily separated and identified on the basis of their retention times. Applying this method to the pharmacologically highly relevant immunoglobulins, we demonstrated for the first time a complete structural assignment and quantitation of neutral and sialylated glycans in single chromatographic runs from SDS PAGE bands. A glycome analysis of only 105 cultured chondrocyte cells revealed a shift from 2,6- to 2,3-sialylation in response to pro-inflammatory cytokine exposure. These results nicely correspond with mRNA expression levels of the respective sialyltransferases as analyzed by our cooperation partner from the medical University Vienna.