Application of Liquid-Liquid Partition Chromatography (LLPC) in the Preparation of Steroid Binding Proteins

Two human serum proteins, i.e. sex hormone binding globulin (h-SHBG) and corticosteroid binding globulin (h-CBG), rat corticosteroid binding globulin (r-CBG), and progesterone binding globulin (PBG) from new guinea pig were purified by the application of three different modes of chromatography. The proteins were purified by affinity chromatography and anion exchange chromatography. Fractions containing the steroid binding proteins were finally purified by liquid-liquid partition chromatography on LiParGel 750 (Merck, Darmstadt, FRG). This Chromatographic sequence clearly separated the steroid binding proteins from other proteins, mainly from serum albumin without a loss of protein and completely retaining the binding affinity towards steroids.