The glycoconjugates in neonate rat eyelids at postnatal day 0 or 1 were examined by lectin histochemistry. Maackia amurensis lectin II, which recognizes sialic acid alpha 2, 3 galactose beta 1, 3 N-acetylgalactosamine (Gal beta 1, 3 GalNAc) or sialic acid alpha 2, 3 galactose beta 1, 4 N-acetylglucosamine, bound to the cell membranes of the epithelial basal cells, suggesting that the glycoconjugates containing these sugar chains are present on their cell membranes. With respect to the binding of the Gal beta 1, 3 GalNAc-specific lectin, jacalin, whose binding is not inhibited by the terminal sialic acid, bound to the cell membranes of the epithelial basal cells, whereas peanut agglutinin, whose binding is inhibited by the terminal sialyl residue, did not bind to their cell membranes. These findings suggest that all the residues of Gal beta 1, 3 GalNAc in the glycoconjugates of their cell membranes are sialylated as the mature form.