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[Purification of Meerrettich-peroxidase by means of affinity chromatography on concanavalin A-agarose].

Michael Wagner

Abstract

Crude preparations of horse-radish peroxidase were purified by means of affinity chromatography on Concanavalin A-agarose. The peroxydase was bound to Concanavalin A, whereas the majority of other proteins of the preparation pass through the column. Subsequently the peroxidase was eluted by means of 1 M sucrose with high purity. The purified enzyme is convenient for the immunoenzyme technique.

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Available abstract

Key concepts: Concanavalin A, Affinity chromatography, Agarose, Chromatography, Peroxidase, Chemistry, Enzyme, Elution