Affinity chromatography of human serum proteins using matrix bound lectin from VISCUM ALBUM L.
Journal/Book: Experientia 35, 161. 1979;
Abstract: The D-galactose specific lectin from Viscum album L. reacts with serumproteins that contain the corresponding D-galactopyranosyl residues. Byaffinity chromatography of human serum on lectin-sepharose IgM, alpha2-macroglobulin, haptoglobin and beta-lipoprotein were quantitativelyretained. Only parts of IgA, IgG and transferrin were retarded. Theother serum proteins are unbounded as albumin, beta 1 A- and beta 1C-globulin. Author.
Keyword(s): CHROMATOGRAPHY-AFFINITY/MT (methods)