The major albumin proteins from pea (Pisum sativum L). Purification and some properties

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Abstract
A scheme is described for the fractionation of pea albumin proteins. By using this scheme, 2 closely related major albumin proteins were isolated and purified to homogeneity. The larger protein, designated PMA-L, has MW .apprx. 53,000 and consists of two 25,000-MW subunits, whereas the smaller, PMA-S, has MW .apprx. 48,000 and contains two 24,000-MW subunits. There was no evidence of mixed dimers of the 2 subunit sizes, despite their close homology as judged by immunological cross-reaction, amino acid composition, N-terminal amino acids, tryptic-peptide mapping and CNBr-cleavage products. Both proteins contained significant amounts of S amino acids. The proteins were located in the soluble cytosol fraction of cotyledon cells and are not significantly degraded on seed germination. Preliminary screening indicates the presence of homologous major albumin proteins in at least 3 different, though closely related, legume species [Lathyrus odoratus, Lens culinaris, Cicer arietinum].