The role of the N-terminus of human alpha(1D)-adrenoceptors was examined by deleting the first 79 amino acids (Delta(1-79)) and epitope-tagging to facilitate immunoprecipitation and detection. Following transfection into HEK293 cells, 6- to 13-fold increases in the density of specific [125I]BE 2254 binding sites were observed for both tagged and untagged Delta(1-79)alpha(1D)- compared to full-length alpha(1D)-adrenoceptors, while agonist and antagonist affinities remained unchanged. In contrast, immunoprecipitation of tagged receptors showed that full-length alpha(1D)-adrenoceptor protein was at least twice as abundant as Delta(1-79)alpha(1D)-adrenoceptor protein. Photoaffinity labelling with [125I]arylazidoprazosin showed much more intense labelling of tagged Delta(1-79)alpha(1D)- than of full-length alpha(1D)-adrenoceptors. Substantial N-linked glycosylation of tagged Delta(1-79)alpha(1D)-adrenoceptors was observed, although full-length alpha(1D)-adrenoceptors contain two consensus glycosylation sites but are not glycosylated. These results suggest that N-terminal truncation of alpha(1D)-adrenoceptors enhances processing of a binding competent form in HEK293 cells; and show a clear dissociation between abundance of receptor protein and density of receptor binding sites.