Helianthinins are storage proteins present in Helianthus annuus seeds, belonging to the 11S globulin family. Here we describe that a fraction of the helianthinins is phosphorylated. This conclusion is supported by different criteria, including identification by matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry of major protein bands revealed with a specific dye for phosphoproteins, anti-phosphoserine antibody and binding to a phosphoprotein affinity matrix. Moreover, we show that the phosphorylation status of helianthinins changes following germination.

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.

Priming of sugarbeet (Beta vulgaris L.) seeds induces increased solubilization of the basic B-subunit of 11-S globulin (a major seed storage protein in sugarbeet). Using a sensitive single-seed ELISA, the soluble and total B-subunit contents of individual untreated and primed sugarbeet seeds were measured. With the untreated seeds, there was a 160-fold range of the soluble B-subunit content among individual seeds. The individual primed seeds also exhibited large variations in their soluble B-subunit content, yet only over a five-fold range. Furthermore, the frequency distributions of soluble B-subunit content were markedly different for the primed and untreated seed populations; the primed seed population exhibited a substantially higher median than that for the untreated seed population. In marked contrast, and as expected from results with pooled seed samples, the distributions of total B-subunit content were superimposed when comparing untreated and primed seed populations.