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The electrophoretic patterns of egg white under the condition of pH 7.8, 0.15μ (phosphate buffer) were obttined by employing the Tiselius apparatus with a cylindrical-lens system constructed by the author.The eleven components, except ovomucin, were reported and discussed by referring to the previous reports. The electrophoretic composition was computed from the patterns and compared with the results of Longsworth, et al. (1940), Bain, et al (1947), Forsyth, et al (1950), and Sorensen (1933-35).There was almost no difference between the three separate layers of egg white.Next, each process of the fractionation of egg white be sodium sulfate according to Kekwick and Cannan was traced electrophoretically. When sodium sulfate was added to egg white to half saturation, a precipitate containing mucin and globulins separated out. It was found electrophoretically, that this precipitate contained an especially large amount of G2-globulin, but a small amount of each globulin remained in the filtrate, Then, almost all of ovalbumin, with a small amount of conalbumin and ovomucoid, was precipitated by the saturation of sodium sulfate. A small amount of each globulin was also precipitated together. When this precipitate was dissolved into distilled watet, the remaining globulins were removed, and ovalbumin was recrystallized by the addition of sodium sulfate.The initially recrystallized albumin was almost pure, electrophoretically. When three recrystallization were repeated, aquite pure ovalbumin was obtained as needle crystals (20-30μ).

Electrophoretic Study of Chicken Egg White and Process of its Fractionation by Sodium Sulfate