A previously established map of the surface epitopes of human chorionic gonadotropin (hCG) served as template for the present study in which we investigated the antigenic surfaces of two glycosylation variants of hCG, i.e. desialylated hCG (asialo-hCG) and deglycosylated hCG (degly-hCG). This map allocates five epitopes to the alpha subunit, five to the beta subunit and four alpha beta epitopes to structures formed only by the alpha/beta heterodimer holo-hCG (Schwarz et al. (1986) Endocrinology 118, 189-197; Berger et al. (1990) J. Endocrinol. 125, 301-309). Here it is described that both variants complied with this template: each of the 14 distinct monoclonal antibodies with which the epitopes of hCG were defined reacted with radiolabeled asialo-hCG and degly-hCG as well and generally bound degly-hCG with greater affinity than hCG. Moreover, every combination of capture and radiolabeled detection antibody that was either compatible or incompatible on unlabeled hCG was so also on unlabeled asialo-hCG and degly-hCG. It thus appears that alterations of the carbohydrate structure of hCG can be associated with a change in affinity between some antibodies and their respective epitopes but not with a loss of an epitope or with a change in the topographical relationships of the 14 epitopes.