Hybrid affinity chromatography of alpha-galactosidase from Verbascum thapsus L

Purification of alpha-galactosidase from the roots of Verbascum thapsus L. was difficult to achieve using conventional methods due to the presence of coloured contaminants. A newly developed procedure, hybrid affinity chromatography, which was based on a mixed matrix separation procedure, using a substrate analogue and an immobilized metal affinity matrix as ligands, respectively, allowed the purification of this enzyme with good recovery. The method should be applicable to other proteins as well.