In order to purify honeysuckle peroxides and study the enzymatic properties and inhibition kinetics,DEAE cellulose DE-52 ion exchange chromatography was used for purification of peroxidase from Lonicera Japonica Thunb prepared preliminarily by three-phase partitioning. Two kinds of peroxidase, HSPⅠ（honeysuckle peroxidaseⅠ）and HSPⅡ（honeysuckle peroxidaseⅡ）, were purified,the specific activity were 3 312.3 U/mg and 564.8 U/mg respectively. The double substrate enzymatic reaction type was PingPong reaction analyzed by the reaction kinetics. Citric acid, Sodium metabisulfite showed irreversible inhibition to Lonicera Japonica Thunb peroxidase, L-cysteine showed reversible inhibition, and L-cysteine was a competitive inhibitor that the inhibition constant K_I was 0.053 mmol/L.