Heterogeneity of subunit composition in lupin globulins. Comparison of proteins from a single seed and from a number of seeds

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Abstract
The subunit compositions of a legumin‐like (globulin 8) and a vicilin‐like protein (globulin 4) extracted from a plurality of seeds and from a single seed both in commercial and in a selected cultivar of Lupinus albus were studied. In the case of globulin 4, a very similar number of bands were observed in SDS‐PAGE, in the protein extracted from a batch of seed and in the same globulin isolated from a single seed. For globulin 8 the SDS‐PAGE pattern showed fewer subunits in the protein from the batch of seeds than in that from a single seed. This is more pronounced in the single seed and in the plurality of seeds of a selected cultivar. Reasons for this behaviour are discussed.