“…The combined use of immunocytochemistry (anti-RF serum), lectins, and specific glycosidades applied in sequence to the same sections led to the following conclusions: (1) the secretory products within the RER are N-linked, high-mannose-type glycoproteins; (2) the products within the apical secretory granules are N-linked, complex-type glycoproteins, with the sequence in the terminal chain of -GlcNac-Galsialic acid; and (3) the apical secretory granules and the pre-RF material share the same immunocytochemical and lectin binding properties (Ferná ndez-Llebrez et al, 1987;Grondona et al, 1994b;Herrera and Rodríguez, 1990;Nualart et al, 1991;Rodríguez et al, 1986Rodríguez et al, , 1987bRodríguez et al, , 1990; S. Rodríguez et al, 1987). Ultrastructural lectin histochemistry has confirmed these observations (Grondona et al, 1994b;Peruzzo et al, 1990;Rodríguez et al, 1986). Core glycosylation of the SCO glycoproteins was confirmed by the disappearance of the Con-A binding sites after the in vivo administration of tunicamycin (Herrera and Rodríguez, 1990).…”