Proteins of aleurone grains isolated from cotyledons ofLupinus luteus L.

Lupin aleurone grains from dry cotyledons contain about 87% of globulin including 57% of proteins solubilized by NaCl solution and 30% by NaOH extractions, and also about 12% of albumin. Activity of acid protease with the optimum at pH 3.6-3.8 was associated with albumin. Albumin was separated by gel filtration on Ultrogel AcA 22 into 3 fractions with mol. m. 179 000, 113 000, and below 100 000, respectively. The component with mol. m. 113 000 prevailed and comprised about 60% of albumin. Globulin was composed mainly of two major components with mol. m. above 364 000 and about 280 000. These correspond to α-and β-conglutin fractions, respectively. γ-conglutin minor globulin fraction of lupin aleurone grains was composed of about 66% glycoprotein. In contrast, about 82% of albumin lack glycosylation. Essentially, globulins in lupin aleurone grains are glycoprotein.