Purification of Prealbumin from Human Serum

Abstract A method is presented by which prealbumin (thyroxine-binding prealbumin; tryptophan-rich prealbumin) may be purified to homogeneity from human serum. The method involves precipitation of contaminating proteins with dilute aqueous phenol, ion-exchange chromatography on DEAE-Sephacel, and gel permeation chromatography on Sephadex G-100. The yield is 25–30%, and the prealbumin is homogeneous by polyacrylamide gel electrophoresis at pH 8.9 and pH 3.6.