Livetin, the major water-soluble protein of hen egg yolk, was found to contain three major components having mobilities of −6.3, −3.8, and −2.1 cm.2 sec.−1 volt−1 at pH 8, µ 0.1, and these have been designated α-, β-, and γ-livetin respectively. The α- and β-livetins were separated and purified electrophoretically after removal of γ-livetin by precipitation from 37% saturated ammonium sulphate or 20% isopropanol. The α-, β-, and mixed livetins resembled pseudoglobulins in solubility but γ-livetin was unstable and this loss of solubility has, so far, prevented its characterization. Molecular weights determined by light scattering, osmotic pressure, and Archibald sedimentation procedure yielded respectively: 8.7, 7.8, and 6.7 × 104 for α-livetin, and 4.8, 5.0, and4.5 × 104 for β-livetin. Under suitable conditions of sedimentation and electrophoresis, egg yolk has been shown to contain three components having the same behavior as the three livetins of the water-soluble fraction.
