Age-related macular degeneration (AMD) is a disease of the central portion of the retina. It is the leading cause of blindness in over-55 population and the third cause of blindness globally, after cataracts and glaucoma. Numerous research projects are devoted to elucidating the etiopathogenesis and identifying potential biomarkers. Glycosylation is the post-translational modification process for proteins. Immunoglobulin G (IgG) is well-studied N-glycoprotein that participates in the homeostatic control of the immune response. The interindividual variation in the glycosylation profile of IgG is affected by the expression of glycan-related genes, epigenetic regulation, as well as constitutional and environmental factors. Glycosylation changes are present in the early acute phase and the development of chronic stages of the disease; therefore, the analysis of the glycan profile of proteins and immunoglobulin G in plasma would be significant in identifying the processes involved in the pathogenesis of AMD. The objective of this study was to compare the glycosylation patterns of total proteins and immunoglobulin G in plasma from different groups of 10,001 Dalmatian subjects with macula degeneration to a relevant control group. The subjects with unilateral and bilateral signs of AMD were elderly people and had dysfunctional lipid metabolism.The multivariate analysis of glycan structures did not produce a significant result in subjects under 55 years of age with macular degeneration. The most significant result regarded lower odds for di-galactylated bi-antennary glycans with core fucose and terminally attached sialic acid [IgG_GP18 (P < 0,009)] in unilateral cases of AMD. The described alterations in glycan structures may indicate a failure of reparative para-inflammatory mechanisms. The most significant result revealed increased odds for tetra-antennary structures with fucosylation of the outer branch grane [DG13 (P < 0,001)], which is a strong indicator of inflammation, in bilateral cases of AMD. Only the increase in tetra-antennary glycans with fucosylation of the outer branch was significantly different between the three subject groups in one category and the control group. This result reveals the limitations of the conducted research due to the cross-sectional nature of the study based on a single measurement of glycan structures from a single available biological sample. Future studies should aim for a more precise evaluation and classification of subjects according to disease phenotype, with continuous clinical monitoring and multiple measurements of glycans in various biological samples.