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Acetone fractionated peroxidase from crude extract of Brassica oleracea leaves (Cabbage) was purified in three steps on chromatographic columns، using Sp-Sepharose، DEAE-Sepharose and Con A-Sepharose. The specific activity of purified main isoenzyme (BOC-POD) is 1887 u/mg protein with RZ: 3.1، which is 172 times more than the RZ of crude extract with 4.3% recovery. The molecular weight of BOC-POD is about 45،000 Dalton. Maximum pH، thermal activity and stability of this purified enzyme are also determined. Km of this isoenzyme was measured by Linewearver-Burk curve for O-dianisidine towards H2O2. This purified enzyme could be used in manufacturing diagnostic kits.