Conglutins are multisubunit, glycosylated, major storage proteins present in Lupinus seeds that self-aggregate in a calcium/magnesium-dependent manner. Two of these globulins exhibit lectin activity. The 210 kDa globulin derived from beta-conglutin that accumulates in Lupinus cotyledons during germination was used as a model protein to establish whether the self-aggregation process is electrostatic in nature or lectin-mediated. This protein binds in a very strong manner to chitin and recognizes a variety of glycoproteins including immunoglobulins G. Several compounds were tested for their inhibitory effect on the cation-dependent self-aggregation process. Sialic acid and phytin were the most effective whereas chitin and mucin were totally ineffective. The inability of the oligosaccharidic side chains of the 210 kDa protein, beta-conglutin and immunoglobulin G to interfere with the aggregation strongly supports the view that Ca/Mg are electrostatically involved in the in vitro self-aggregation of Lupinus globulins. The results suggest that calcium and magnesium ions are also electrostatically involved in vivo in the macromolecular aggregation of legume seed storage proteins, ensuring their efficient packing inside the protein storage vacuoles. This mechanism is responsible for the typical insolubility of legume globulins in water.