Primary structure and polymorphism of 2S albumins from seeds of Andean lupin (Lupinus mutabilis Sweet) |
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Authors: | B. P. Salmanowicz |
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Affiliation: | Institute of Plant Genetics, Polish Academy of Sciences, ul. Strzeszy?ska 34, PL-60-479 Pozna?, Poland e-mail: bsal@igr.poznan.pl, PL
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Abstract: | 2S albumins were isolated from seeds of Andean lupin (Lupinus mutabilis Sweet) by buffer extraction, ammonium sulphate precipitation and ultrafiltration followed ion-exchange and reversed-phase HPLC. The 2S albumin preparation (LM2S) contained eight albumins. The complete amino acid sequences of small and large subunits of three major albumins (LM2S-4, -5 and -6) were determined by automated Edman degradation of S-pyridylethylated polypeptides and peptides obtained from them by enzymatic digestions. The small subunit of the dominant 2S albumin (LM2S-4) contains 39 amino acid residues and has a molecular mass of 4731 Da. The large subunit of LM2S-4 contains 74 amino acid residues (molecular mass=8708 Da). Two 2S albumin isoforms (LM2S-4 and -6) are due to the expression of two distinct genes; LM2S-6 isoform has eight amino acid replacements when its sequence is compared with the sequence of LM2S-4. The LM2S-5 isoform contains an identical small subunit to LM2S-4, and has in comparison with LM2S-4 two additional amino acid residues at the N-terminus of the large subunit. The amino acid sequences of 2S isoforms from L. mutabilis showed high homology (78–83% identity) with 2S albumins from different Old World Lupinus species. Received: 15 December 1998 / Revised version: 9 February 1999 |
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Keywords: | 2S Albumins Lupin Lupinus mutabilis Amino acid sequences Polymorphism |
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