Abstract
All the main globulins in the seeds ofLupinus Albus are oligomeric glycoproteins. Legumins (33%) consist of two similar protein molecules which contain protomers linked by disulphide bridges. They result from a partial proteolytic breakdown of an original polypeptide chain. Vicilins (44%) consist of four similar protein molecules with several protomers linked together by non-covalent bonds. Globulin 1 (6%) has a native M.W. of 199 kd and is formed by four 45.0 kd subunits consisting of two smaller protomers (28.0 and 16.0 kd) linked by -S-S- bonds. Globulin 9b (12.5%) has the lowest M.W. (44.0 kd) and is made up of three protomers, two of which are linked by disulphide bonds.
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References
Duranti M, Restani P, Poniatowska M, Cerletti P (1981) The seed globulins ofLupinus albus. Phytochem 20:2071–2075
Restani P, Duranti M, Cerletti P, Simonetti P (1981) Subunit composition of the seed globulins ofLupinus albus. Phytochem 20:2077–2083
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Duranti, M., Cerletti, P. Subunit composition of proteins from seeds of Lupinus albus. Plant Food Hum Nutr 33, 135–138 (1983). https://doi.org/10.1007/BF01091299
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DOI: https://doi.org/10.1007/BF01091299