Lipoxygenase from Shelduck muscle was purified by the combination of ammonium sulfate precipitation,anion exchange chromatography and gel filtration chromatography. The purified Shelduck LOX was electrophoretically pure and with the specific activity of 85 714. 3U / mg. Its molecular weight was about 62 kDa,which was smaller than that of the LOX from soybean. Further investigation revealed that the optimal temperature and pH value of shelduck LOX were 30℃ and 6. 0 respectively,which were quite different from that of Soybean LOX. The thermal and pH stability of Shelduck LOX were also better than that of soybean LOX. Zn2 +,Ca2 +had a strong activating effect on shelduck LOX,but Mn2 +was a strong inhibitor.