Electrophoretic Separation of Conjugated Bilirubin on Paper

Abstract

IN previous experiments¹ the 0.02 M phosphate buffer of pH 6.8 was used for electrophoresis of bile pigments on paper. Under these conditions (in the absence of proteins) the conjugated bilirubin migrating anodically separates from the unconjugated bilirubin which remains on the starting line. The presence of bile salts clearly influences this separation. Purified preparations² of conjugated bilirubin which are devoid of bile salts migrate in the form of a tail beginning just from the starting line. If bile salts are present a sharply denned zone of conjugated bilirubin separates, migrating in front of the bile salts. The velocity of migration of this zone in the presence of bile salts is considerably higher than the rate of migration of pure preparations of the pigment.