Purification of retinol-binding protein from serum and urine by affinity chromatography

A new method for the purification of retinol-binding protein from urine and serum is described. The method is based on the reversible binding of retinol-binding protein to retinoic acid linked to Sepharose and prealbumin linked to Sepharose. The yield is comparable to conventional methods using ion exchange and gel filtration and the product is an apo retinol-binding protein of high purity. The product has the same electrophoretic mobility and molecular weight and the same ability to interact with retinoic acid and prealbumin as retinol-binding protein prepared by conventional methods.