Peroxidase was purified in a single step using 4-amino benzohydrazide affinity chromatography from red cabbage (Brassica oleracea var. capitata f. rubra), and some important biochemical characteristics of the purified enzyme were determined. The enzyme, with a specific activity of 3,550 EU/mg protein, was purified 120.6-fold with a yield of 2.9 % from the synthesized affinity matrix. The molecular weight of the enzyme was found to be 69.3 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme exhibited maximum activity at pH 7.0 and 30 A degrees C. For guaiacol substrate, the K (m) and V (max) values were found as 0.048 mM and 1.46 EU/mL/min, respectively. Additionally, the IC50 and K (i) values for 4-amino benzohydrazide were calculated to be 1.047 and 0.702 A +/- 0.05 mM, respectively, and 4-amino benzohydrazide showed noncompetitive inhibition.