Binding of divalent metal ions to hepatic soluble β-galactoside binding lectin was studied using electron spin resonance (ESR) spectroscopy. The Mn2+ bound to hepatic lectin could be displaced by Mg2+, Cu2+, Ni2+ and Ca2+ but not by Sr2+. As the ionic radii of Mg2+ (0.65 Å), Cu2+ (0.73 Å) and Ni2+ (0.72 Å) are appreciably smaller than Ca Mn2+ binding site is more accessible to Mg2+, Cu2+, and Ni2+ as compared to Ca2+, the ionic radius of Mn2+ being 0.80 Å. Sr2+ with an ionic radius of 1.13 is thus unable to displace bound Mn2+. Surprisingly, the presence of specific sugars like α-lactose, or α-d-galactose facilitated the displacement of bound Mn2+ by metal ions whereas non-specific sugars, i.e. α-d-glucose, β-d-fructose and α-d-ribose had no effect. It appears that minor perturbations in the saccharide binding site significantly affect the ability of the metal binding site to ligate bivalent metals.