作　　者： ; ; ; ;

机构地区： 扬州大学农学院植物保护系

出　　处： 《昆虫学报》 2005年第5期649-654,共6页

摘　　要： 采用40%硫酸铵沉淀、Blue Sepharose CL-6B亲和层析和Phenyl Sepharose CL-4B疏水层析等方法,从亚洲玉米螟Ostrinia furnacalis(Guenée)幼虫血清中分离纯化了酚氧化酶原.酚氧化酶原全酶相对分子量约为158 kD,亚基相对分子量约为80 kD和78 kD.酚氧化酶原为糖蛋白,该酶原易被0.1 mmol/L CPC(氯代十六烷基吡啶)、50%甲醇、1 mg/mL昆布多糖和1 mg/mL胰蛋白酶激活.该酶反应的最适pH为7.0,最适温度为25～30℃,Ca2+和Mg2+可增强该酶的活性. The prophenoloxidase （PPO） was purified from the hemolymph of the larvae of Ostrinia furnacalis （Guenre） by sequential use of precipitation in 40% saturation ammonium sulfate, the affinity chromatography of Blue Sepharose CL-6B and Phenyl Sepharose CL-4B. The relative molecular weight of prophenoloxidase was 158 kD, and the molecular weight of two subunits was 80 kD and 78 kD, respectively. The prophenoloxidase was glycoprotein and could be activated by 0.1 mmol/L cetylpyridmium chloride （CPC）, 50% methanol, 1 mg/mL laminarin and 1 mg/mL trypsin. The optimum pH was 7.0 and the optimum temperature 25-30℃ for prophenoloxidase activity, which could be significantly stimulated by Mg^2＋ and Ca^2＋ .

关 键 词： 亚洲玉米螟 血清 酚氧化酶原 分子量 最适 最适温度 酶活性

领　　域： [生物学]