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.
D002846:Chromatography, Affinity / Q000379:methods; D005697:Galactosides; D006023:Glycoproteins / Q000097:blood*; D006801:Humans; D037102:Lectins; D014784:Mistletoe / Q000032:analysis; D037121:Plant Lectins; D010946:Plants, Medicinal
D005697:Galactosides; D006023:Glycoproteins; D037102:Lectins; D037121:Plant Lectins