[Blood retinol-binding protein: its isolation and properties].

Ion-exchange chromatography on DEAE-cellulose, preparative electrophoresis in polyacrylamide gel and gel-filtration on Sephadex G 100 were used to isolate and purify retinol-binding protein (RBP) from the blood serum of chickens. The molecular mass of RBP was equal to 19 500. Excitation and fluorescence spectra had maxima at 340 and 475 nm, respectively. The combined scheme of rabbits' immunization with purified RBP enabled one to obtain an active enough monospecific antiserum upon minimal losses of antigen. The purity of RBP obtained was confirmed both biochemically and immunologically.