Immunoglobulin gamma is the most abundant antibody present in serum. Its functions are regulated by glycosylation which is a type of posttranslational protein modification. IgG N-glycosylation describes oligosaccharides linked to the polypeptide chain through the asparagine residue 297. Sugar moieties such as fucose, galactose or sialic acid mediate IgG’s anti-inflammatory or pro-inflammatory properties by affecting the binding of the Fc region on IgG to activating or inhibitory Fc gamma receptors located on immune cells. Due to the fact that the physiological state and stress have a great impact on IgG N-glycosylation, research of N-glycome profiles can result with discovering novel biomarkers. After mice, rats are the second most used animal model in scientific research. Characterization of IgG N-glycome of a healthy rat can be compared to physiologically altered states such as disease, or it can be used to analyze drug mechanisms of action. N-glycome analyzes are technically very challenging and therefore strongly depend on implementing precise and sensitive methods for isolation, purification and identification of N linked glycans. In this thesis, isolation of IgG from rat serum was performed by affinity monolithic chromatography. Advantages of using monolithic columns include shorter time of analysis, narrower detection peak and, greater physical stability at higher pressures. Immobilized protein L was used as a ligand due to high affinity for IgG kappa light chains. Confirmation of IgG isolation was performed by MALDI-TOF mass spectrometry. A comparison between protocols for in-gel tryptic digestion was carried out wherein a protocol developed by Shevchenko et al.. was compared with an in-house protocol developed at the Department of Biotechnology. The comparison showed that the protocol developed Shevchenko et al. achieved more reliable results compared to the results obtained through the in-house developed protocol. N-glycan identification was performed using MALDI-TOF MS. Identification of glycans largely depends on the derivatization process. Derivatization protocols used in this thesis have not achieved the desired technical reproducibility for all samples and glycans from only two samples were successfully identified. In the future, better protocol optimization could identify the complete N-glycan profile of IgG.