The structure of lupine seed proteins

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Abstract
Lupine globulins (87% of total seed proteins) can be grouped into 3 categories: vicilin‐like proteins (44%), legumin‐like proteins (33%) and other globulins (23%). The four vicilins. namely globulins 4, 5, 6 and 7, have a M. W. ranging between 143 and 335 ‐ 103 g ‐ mol−1; they all contain covalently linked carbohydrate and consist of several protomers of some M. W. in the various fractions, the heaviest of which has a M. W. of about 60 ‐ 103 g ‐mol1. No disulphide bonds link these protomers together. Legumins, i. e. globulins 8 and 9a. consist of acidic and basic subunits linked by S S bonds. Also the legumins are glycoproteins. the carbohydrate moiety being covalently bound only to the acidic subunits. They have a M. W. ranging between 52 and 36 ‐ 103 g ‐ mol1, whereas the basic subunit has a M. W. of 19 ‐ 103 g ‐ mol1. Globulin 8 is present in two forms A and B, of respectively 188 and 349 ‐ 103 g ‐ mol−1. Globulin 1 (6% of total globulins) is made up of disulphide bound protomers of 16 and 28 ‐ 103 g ‐ mol−1. Only the heavy protomer is glycoxylated. Globulin 9b (12.5% of total globulins) has the lowest M. W. (44 + 103 g ‐ mol1) and it is formed by disulphide bound protomers of 11 and 13 + 103 g ‐ mol1.