Primary structure of 2 S albumin from seeds of Lupinus albus
1997
Salmanowicz, B.P. | Weder, J.K.P.
The 2 S albumin from the seeds of white lupin was purified by ammonium sulfate precipitation and ultrafiltration followed by anionexchange and reversed-phase HPLC. The complete amino acid sequences of the large and the dominating small subunit were determined by automated Edman degradation of the reduced and S-pyridylethylated polypeptides and of their enzymatic fragments. The small subunit of the 2 S albumin (a) consists of 37 amino acid residues resulting in a molecular mass M(r) of 4407. The large subunit (b) contains 75 amino acid residues (M(r) = 8827). The two polypeptide chains are linked by two interchain disulfide bonds. In addition, the large polypeptide contains two intrachain disulfide bridges, and one free sulfhydryl group. A high degree of homology (88%) exists between the primary structure of the 2 S albumin from L. albus and that of a comparable 2 S protein from L. angustifolius, designated conglutin delta.
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