The basic B-subunit of the seed storage protein 11-S globulin (an 11-S-legumin type protein) is the major polypeptide in soluble protein extracts from primed sugarbeet (Beta vulgaris L.) seeds. In contrast, only a small amount of this protein is present in corresponding extracts from untreated dry mature seeds. Here, and as for all 11-S globulins described so far, the B-chain is linked to other polypeptide(s), corresponding most presumably to an acidic A-chain, through the formation of disulphide bridge(s). Polyacrylamide gel electrophoretic analyses of total and soluble protein extracts from untreated and primed seeds strongly indicate that this priming-induced solubilization of the B-chain resulted from an endoproteolytic attack on the A-chain. Microscopical immunolocalization showed a uniform distribution of the 11-S globulin B-chain over the protein bodies of the embryonic cells from the untreated seeds. For the primed seeds, however, the B-subunit of 11-S globulin diffused out of the protein bodies and invaded the cytosolic compartment. This phenomenon occurred independently of the manner of priming, being observed with hydroprimed and osmoprimed seeds, as well as with sugarbeet seeds that had been primed by a prehydration treatment. Quantitative analyses of the amounts of soluble 11-S globulin B-chain have enabled the priming of sugarbeet seeds to be optimized.