Hybrid affinity chromatography of α-galactosidase from Verbascum thapsus L

Purification of α-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 substr...

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Veröffentlicht in:Journal of Chromatography A 1998-05, Vol.808 (1), p.133-139
Hauptverfasser: Bom, Isaac, van Wassenaar, Dick, Boot, Johan
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container_title Journal of Chromatography A
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creator Bom, Isaac
van Wassenaar, Dick
Boot, Johan
description Purification of α-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.
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subjects alpha-Galactosidase - isolation & purification
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Chromatography, Affinity - methods
Concanavalin A
Electrophoresis, Polyacrylamide Gel
Enzymes
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Galactosidase
Hydrolases
Isoelectric Focusing
Isoelectric Point
Plant Lectins
Plant Roots - enzymology
Plants - enzymology
title Hybrid affinity chromatography of α-galactosidase from Verbascum thapsus L
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