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Subunit structure of Vicia faba legumin and implications for the improvement of protein quality

✍ Scribed by Horstmann, C. ;Müntz, K.

Publisher
John Wiley and Sons
Year
1986
Tongue
English
Weight
567 KB
Volume
30
Category
Article
ISSN
0027-769X

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✦ Synopsis

Legumin, the main storage protein of Viria faba seeds. consists of the two different subunit types A and B.

Each subunit is composed of two polypeptide chains, one acidic (2) and one basic (p) linked by disulphide bridges. In each subunit type specific a-P-pairs occur. in type A 3-as well as 8-polypeptides contain methioninc, whereas in both the constituent polypeptides of type B subunits methionine is lacking. Since the specific r-B-pairs reflect their origin from a common precursor and hence from a single gene for each subunit, it seems worthwhile to look for Vicia varieties containing an increased ratio of type A/B subunits and therefore a legumin with a higher content of the nutritionally limiting amino acid methionine. Results of such a screening are presented.

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