Soybean lipoxygenase 2 was purified by the combination of ammonium sulfate fractionation, affinity chromatography on linoleate-aminohexyl Sepharose 4B and DEAE-cellulose chromatography. Purification of lipoxygenase 2 through affinity chromatography resulted in 6-fold purification and the yield of 91%, while lipoxygenase 1 was retrogressed and recovery was only 15%. Overall purification of lipoxygenase 2 was 32.4 folds and the yield was 28.5%, respectively. The purified enzyme preparation was almost homogeneous electrophoretically. When the lipoxygenase 2 preparation was incubated with arachidonic acid, and subsequently reduced with sodium dithionite, a material from ether extract of the reaction mixture seemed to have some of prostaglandin $F_{2{alpha}}$, which was identified through thin layer chromatography.