[Sweet lupine (Lupinus luteus, var. Aurea/Weico and Lupinus albus, var. Multolupa) proteins. II. Separation by electrophoresis].

The albumins and globulins extracted from Lupinus luteus var. Aurea/Weico and Lupinus albus var. Multolupa defatted flour samples were analyzed by polyacrilamide gel electrophoresis. The purpose was to determine the percentage distribution of pattern in the electrophoretograms and the relative mobility values of protein. The L. luteus albumins densitogram showed six fractions, two of them, No. 2 and No. 4, represented 58.1% of the total. On the other hand, the globulins densitogram revealed five fractions, numbers 1, 2 and 3 representing 90.7%. The densitogram of peak I from Sephadex G-100 globulins filtration indicated two fractions similar to those number 1 and 2 of the total globulins, showing low relative mobility values (from 0.26 to 0.39). The L. albus albumins resolved in four fractions, with No. 2 being the most prevalent (54.3%). In regard to the L. albus globulins, these showed five fractions identical in distribution with those of peak I, fraction 2 appearing as the most important (48.2%). It was found that Sephadex G-100 did not perform a good separation. As to the relative mobility values of globulins, fractions 2 and 3 were the most prominent (relative mobility of 0.35 and 0.48, respectively). It may be concluded that L. luteus albumins presented more components but with lower relative mobility values than those of L. albus. As for the globulins from both lupine flour samples, the gel separated fractions were classified in two groups of components, those of high and of low relative mobility.