Antibodies play a central role in molecular mechanisms of immune response. The main and most common antibody in blood plasma is immunoglobulin G (IgG). IgG consists of two types of polypeptide chains: heavy (approximately 50 kDa) and light chain (approximately 25 kDa). Each IgG molecule consists of two heavy and two light chains (total molecular weight of approximately 150 kDa). Glycosylation is of great importance for proper functioning of IgG. Each heavy chain carries a covalently bonded bi-antenary N-glycan on the asparagine residue 297. These oligosaccharides have structural and functional importance for immunoglobulin G and its effector functions. Normal synovial joints contain a cavity filled with synovial fluid secreted by the synovial membrane. Synovial fluid is a viscous liquid that has a lubricating and metabolic function within a joint. Maintaining normal composition of synovial fluid is necessary for homeostasis of a joint. Rheumatoid arthritis (RA), which affects approximately 1% of the population, represents an autoimmune attack primarily directed to synovial membranes of synovial joints. The purpose of this paper is to develop a method for IgG N-glycan analysis from synovial fluid as an important biological sample in the study of rheumatoid arthritis. IgG was isolated from synovial fluid by immunoprecipitation using protein G beads, and purification conditions were optimized. N-glycans were released from IgG, labeled and analyzed by UPLC. The developed method will be used in further research of the association of rheumatoid arthritis and IgG N-glycans, preferably in a form that allows high-throughput analysis of a large number of samples.