We have examined the interactions of the membrane-bound enzymes, 5'-nucleotidase and acetylcholinesterase from bovine tissues with lectins and shown that glycosylation contributes significantly to the polymorphism of these enzymes, in a tissue-specific manner. Lectins which bind 5'-nucleotidase also inhibit its catalytic activity to various degrees. We found different specificities with 5'-nucleotidases from various cell types: for example lymphocyte 5'-nucleotidase did not interact with wheat germ agglutinin, in contrast with 5'-nucleotidases from hepatocyte and caudate nucleus membranes. Treatment with glycohydrolases, alpha-D-mannosidase and neuraminidase, suggested that the latter enzymes possess sialic residues which are absent in the lymphocyte enzyme. Interactions of acetylcholinesterase with lectins were demonstrated by sedimentation analysis and binding to immobilized lectins, but its activity was generally not affected. A notable exception was lymphocyte acetylcholinesterase which was inhibited by the fucose-binding Ulex europeus agglutinin. This inhibition was relieved by alpha-L-fucose but not by alpha-D-fucose and reduced after treatment with alpha-L-fucosidase. In addition this enzyme differs from acetylcholinesterases from other tissues by its higher Km value, although it appears immunologically equivalent. The different forms of acetylcholinesterase from the same tissue may differ in their interactions with lectins. In muscle for example G4 carries carbohydrate chains of the complex type whereas G1 appears to possess only the high mannose type. We discuss the possible relationships between these forms.