Glycosylations are considered the most abundant, but also the most complex form of co- and post-translational modifications. Their huge structural and functional diversity renders their analysis rather challenging, as addressed by the present thesis with the validation of two new analytical methods focussing on the electrophoretic separation of glycoproteins in liquid- and gas-phase. Therefore, intact glycoproteins as well as their interactions with lectins were qualitatively and quantitatively investigated by microchip capillary gel electrophoresis (MCGE) and on a nano electrospray gas-phase electrophoretic mobility molecular analyzer (nES GEMMA) instrument. For glycoprotein analysis MCGE demonstrated high sensitivities, high accuracy in quantitation, and a high reproducibility in sizing, i.e. molecular weight (MW) determination. This makes it a good rapid and easy-to-use alternative to the more elaborate sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Deviations in sizing could be observed with both techniques, SDS-PAGE and MCGE, in comparison to mass spectrometric-derived values. Especially in the case of MCGE, they increased in accordance to the degree of glycosylation. Nevertheless, the combination of MCGE with magnetic bead-based lectin affinity enrichment enabled the targeted analysis of glycoproteins from complex biological samples with high selectivity. Validation of the developed strategy with human serum and mycelia extract of the fungus Trichoderma atroviride demonstrated the selective enrichment of glycoproteins. However, the existence of an unspecific binding between the sample and the beads themselves was revealed, too. Affecting glycoproteins, these unspecific interactions can challenge any lectin-based specificity experiment. SDS-PAGE analysis followed by a proteomic approach revealed these results and enabled in addition the identification of two putative glycoproteins for the only fairly studied glycoproteome of Trichoderma atroviride. Based on a size / MW correlation nES GEMMA, on the other hand, allowed MW determinations of the employed glycoproteins and lectins in very good agreement to mass spectrometric values. Operating at ambient pressure and with non-denaturing electrolyte solutions, the system even enabled the analysis of the weak lectin-glycoprotein interactions while maintaining the biological structure of the complex. Interaction studies were performed in regard to binding specificities and affinities towards selected glycoproteins. Results were additionally compared to capillary electrophoresis-on-a-chip-derived data. Next to mere detection, the non-covalent biospecific complex after size-separation could also be sampled onto nitrocellulose membrane with the nES GEMMA device. Subsequent identification by an immunological assay further proved the intact native structure of the analytes throughout the nES process, the gas-phase separation, and even the electrostatic sampling. Consequently, nES GEMMA is a promising platform for the analysis of the weak glycoprotein-lectin interactions specifically with a straightforward sample preparation, a label-free and chemical-nature independent detection, and a simplified data interpretation as only singly charged species are regarded.