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Variation in the Sizes of Both Large and Small Disulphide-Linked Subunits of Legumin in Representatives of Vicieae and Cicer

1982; Elsevier BV; Volume: 107; Issue: 1 Linguagem: Inglês

10.1016/s0044-328x(11)80005-x

0044-328X

Franklin Vairinhos, David R. Murray,

Botanical Research and Chemistry

The distribution of seed globulins has been studied in several members of Vicieae, namely Vicia faba L., Lens culinaris Medik., Lathyrus odoratus L. and Pisum sativum L., and compared with seed globulins of three species of chickpea: Cicer arietinum L., C. reticulatum Ladiz. and C. echinospermum Davis. Globulin samples were analysed using pore-gradient polyacrylamide gel electrophoresis, and their constituent polypeptides examined by disc gel electrophoresis after dissociation with SDS in either the absence or presence of 2-mercaptoethanol to reduce disulphide bonds. The disulphide-linked polypeptides comprising legumin varied in size from 57,000 (36,000 + 21,000) daltons up to 71,000 (50,000 + 21,000) daltons. Of the nine different pairs of disulphide-linked polypeptides detected belonging to legumin, none was held in common by all the Vicieae, and only one was held in common by all three species of Cicer and any member of Vicieae: that of 62,000 (41,000 + 21,000) daltons was also prominent in Lens culinaris. Differences were observed in the sizes of both large and small subunits in most of the Vicieae, but only in the size of the large subunit in all three species of Cicer. The maximum number of legumin components coexisting in a single genotype was found to be four for both wild chickp as and three for most members of Vicieae and C. arietinum.