The purification of horseradish peroxidase by affinity chromatography on Sepharose-bound concanavalin A

Abstract This report describes the use of affinity chromatography on Sepharose-bound concanavalin A for the purification of horseradish peroxidase. Samples of horseradish peroxidase with A 403 : A 280 ratios ranging from 0.62 to 2.45 were purified to A 403 : A 280 ratios ranging from approximately 2.8 to 3.1 with the recovery of 73% or more of the enzymatic activity. Characterization of the purified horseradish peroxidase showed an increased enzymatic activity with respect to both absorbance at 403 nm and protein content.