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研究表明：非亲和性稻瘟菌侵染诱导的水稻过氧羟基脂肪酸羟化环氧化酶（Ｐｅｒｏｘｙｇｅｎａｓｅ，ＰＯＧ）是一种膜蛋白，必须有界面活性剂存在时，才能游离出来。本研究在详细探索了ＰＯＧ的抽提条件和层析条件后，初步建立了ＰＯＧ的如下纯化方法：首先采用非离子界面活性剂选择抽提ＰＯＧ等膜蛋白；并通过硫酸铵盐析收集ＰＯＧ活性组分；然后利用目标蛋白等电点进行阳离子交换层析；根据界面活性剂对目标蛋白在ＤＥＡＥ－Ｓｅｐｈａｒｏｓｅ层析柱吸附的影响，进行阴离子交换层析。通过以上步骤，从稻叶中纯化了稻瘟菌诱导的ＰＯＧ，经ＳＤＳ－ＰＡＧＥ检测，ＰＯＧ为单链多肽，分子量约４７ｋＤ左右。
The results showed that the non-inactivated Magnaporthe grisea rice induced peroxidase (POG) is a membrane protein that must be released in the presence of a surfactant. In this study, the extraction conditions and chromatographic conditions of POG were explored in detail. Purification methods of POG were preliminarily established as follows: Firstly, non-ionic surfactants were used to selectively extract membrane proteins such as POG; POG activity was collected by ammonium sulfate salting-out Then, the target protein isoelectric point was used for cation exchange chromatography. According to the influence of the surfactant on the adsorption of the target protein on the DEAE-Sepharose column, the anion exchange chromatography was performed. Through the above steps, the POG induced by Magnaporthe grisea was purified from rice leaves, and the POG was single-stranded polypeptide by SDS-PAGE. The molecular weight was about 47kD.