Abstract
The D-galactose specific lectin fromViscum album L. reacts with serum proteins that contain the corresponding D-galactopyranosyl residues. By affinity chromatography of human serum on lectin-sepharose IgM, α2-macroglobulin, haptoglobin and β-lipoprotein were quantitatively retained. Only parts of IgA, IgG and transferrin were retarded. The other serum proteins are unbounded as albumin, β1A− and β1C.