Glycosylation is one of the most common and complex posttranslational modifications of proteins in eukaryotic cells and is essential for all forms of multicellular life. Studies on basic characteristics and natural variations of N-glycosylation profiles of total plasma proteins and immunoglobulin G have shown that age, sex, reproductive cycle, environmental influences and lifestyle habits contribute to the variation of human glycome. In a given physiological state, the N-glycosylation profile is highly reproducible, however, due to aging or disease, the glycosylation processes are altered and consequently noticeable changes occur in the glycosylation profile. Changes in the glycosylation profile are in a strong correlation with chronological age and some changes also show sex dependance. This master thesis analysed glycosylation changes based on gender differences in a cohort of young healthy people. Since the majority of comorbidities and chronic health changes, which consequently influence glycans, usually start developing in thirties and/or forties and gradually worsen with age, we made the assumption that participants of this experiment (young healthy people in their twenties) have not yet developed mentioned health issues. Therefore, the glycan changes noticed in this experiment would mostly result from gender differences. Plasma samples of 88 young healthy attendees, aged between 20 and 33 years were used in the study. Using HILIC-UPLC method, N-glycan profiles of total plasma proteins and immunoglobulin G were analyzed. Obtained data was statistically analyzed according to gender using the Mann-Whitney test for independent samples. Statistically significant differences were found in glycosylation profiles of total plasma proteins and IgG, with more pronounced differences occurring in the IgG glycosylation profile. The most significant differences found in the glycosylation profile of total plasma proteins include an increase of agalactosylated glycan structures, structures containing anntenary fucose and highly branched glycan structures in males and an increase of digalactosylated and monosialylated glycan structures in females. In the glycosylation profile of immunoglobulin G an increase of agalactosylated glycan structures was shown in male population, while an increase of digalactosylated and sialylated glycan structures was shown in the female population. The obtained results confirm previous literature findings, with this experiment showing detailed, mostly gender-based differences in N-glycome of total plasma proteins and IgG of young healthy people.