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

  • 1 January 1975
    • journal article
    • abstracts
    • Vol. 34  (8) , 1429-31
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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