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Affinity chromatography of human serum proteins using matrix bound lectin from Viscum album L
Experientia
|February 15, 1979
Abstract:
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.