Affinity chromatography of human serum proteins using matrix bound lectin from Viscum album L.

The D-galactose specific lectin from Viscum album L. reacts with serum proteins that contain the corresponding D-galactopyranosyl residues. By affinity chromatography of human serum on lectin-sepharose IgM, alpha 2-macroglobulin, haptoglobin and beta-lipoprotein were quantitatively retained. Only parts of IgA, IgG and transferrin were retarded. The other serum proteins are unbounded as albumin, beta 1 A- and beta 1 C-globulin.