Affinity chromatography of human serum proteins using matrix bound lectin fromViscum album L.
- 1 February 1979
- journal article
- Published by Springer Nature in Cellular and Molecular Life Sciences
- Vol. 35 (2) , 161
- https://doi.org/10.1007/bf01920586
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.Keywords
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