PREPARATION AND MOLECULAR WEIGHT OF γ-LIVETIN FROM EGG YOLK

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Abstract
A 20% solution of egg yolk in ammonium sulphate at 16% of saturation was centrifuged to float the low density components and the γ-livetin was then precipitated from the subnatant with ammonium sulphate at 40% of saturation. The precipitate was dissolved and reprecipitated several times with ammonium sulphate at 34% of saturation before ether extraction. γ-Livetin prepared in this way contained only a small amount of a heavier component. On purification γ-livetin has the solubility behavior of a euglobulin but loses its solubility irreversibly on prolonged dialysis against water or on freeze-drying. It can be preserved for reasonable periods as a precipitate in saturated ammonium sulphate solution. γ-Livetin has an anomalous sedimentation behavior, the sedimentation rate increasing sharply over a short range of protein concentration. A molecular weight of 1.5 × 105and an axial ratio of about 8 were obtained from sedimentation and diffusion measurements. Other methods gave higher values but are considered less reliable.

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