Isolation and partial characterization of retinol-binding protein from chicken plasma

A simple rapid three-step procedure for the isolation of pure retinol-binding protein from chicken plasma is described. The method comprises DEAE-cellulose chromatography followed by preparative disc gel electrophoresis and final purification by Sephadex G-100 gel filtration. Amino acid analysis showed that there is only a general similiarity between this retinol-binding protein and that obtained from human or rat sources. The molecular weight, which was estimated to be 19 000, is similar to that of rat retinol-binding protein.