The present work describes the purification and characterization of peroxidase from the medicinal plant, Amsonia orientalis, for the first time. The activity recovery for peroxidase was 162% with 12.5-fold purification. Optimal purification parameters were 20% (w/v) (NH4)(2)SO4 saturation at pH 6.0 and 25 degrees C with 1.0:1.0 (v/v) ratio of crude extract to t-butanol ratio for 30 min. The molecular mass of the enzyme was found to be ca. 59 kDa. Peroxidase showed K-m values of 1.88 and 2.0 mM for pyrogallol and hydrogen peroxide, respectively. FeSO4, CuSO4, HgCl2, MnSO4 and MgSO4 did not inhibit the enzyme activity.