title: Purification of human plasma retinol-binding protein by hydrophobic interaction chromatography.
abstract: Human plasma retinol-binding protein has been purified to homogeneity by a simple method that requires an ammonium sulfate fractionation, a hydrophobic interaction chromatography on phenyl-Sepharose, which dissociates the complex between retinol-binding protein and its carrier, transthyretin, and a gel filtration on Sephadex G-50. The yield of pure protein is comparable or higher than that obtained with the more complex procedures previously reported.
mesh_terms: D002845:Chromatography / Q000379:methods; D002850:Chromatography, Gel; D004589:Electrophoresis, Disc; D006801:Humans; D012177:Retinol-Binding Proteins / Q000302:isolation & purification*; D054839:Retinol-Binding Proteins, Plasma; D012685:Sepharose / Q000031:analogs & derivatives
chemical_list: D012177:Retinol-Binding Proteins; D054839:Retinol-Binding Proteins, Plasma; C033452:Phenyl-Sepharose CL-4B; D012685:Sepharose