Affinity chromatography of human serum proteins using matrix bound lectin fromViscum album L.期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

Affinity chromatography of human serum proteins using matrix bound lectin fromViscum album L.

Authors:	P. Ziska H. Franz

Affiliation:	(1) Staatliches Institut für Immunpräparate und Nährmedien, Klement-Gottwald-Allee 317-321, DDR-112 Berlin-Weissensee, (German Democratic Republic)

Abstract:	Summary 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, ₂-macroglobulin, haptoglobin and -lipoprotein were quantitatively retained. Only parts of IgA, IgG and transferrin were retarded. The other serum proteins are unbounded as albumin, ₁A– and ₁C.

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