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In the present study, we examined mollecular forms of urinary prostate-specific antigen (PSA), focusing on its structural complexity in general and specifically on its microheterogeneity in relation to benign prostatic hyperplasia (BPH). Gel filtration, ion-exchange chromatography, and lectin-affinity chromatography were used to characterize PSA. In comparing the binding pattern of PSA isoforms, moderate changes were observed in the relative abundance of distinct molecular subpopulations separated on lectin-affinity columns. They may be related to alteration in the position and type of linkage of fucose or sialic acid, as well as to modification of the trimannosyl core by branching of the PSA oligosaccharide chain

Molecular forms of human prostate-specific antigen in urine of subjects with benign prostatic hyperplasia