THE PURIFICATION OF HAPTOGLOBIN

Abstract

A method for preparing haptoglobin in highly purified form from human serum is described. The serum is acidified to pH 4.6 and deionized by gel filtration. Under these conditions haptoglobin is selectively adsorbed from serum by diethyl-aminoethyl-cellulose. The protein is eluted with a dilute solution of sodium chloride, and impurities are removed by fractionation with ammonium sulphate. A partial purification of serum cholinesterase can be obtained by a similar method.