鸭肝过氧化氢酶的分离纯化及部分性质研究

Isolation and Purification Catalase from Anas platyrhynchos Liver and Analysis of Some Its Properties

新鲜鸭肝经匀浆、磷酸缓冲液抽提、硫酸铵分级沉淀、DEAE-Sepharose离子交换层析、Sephacryl S-200凝胶过滤层析，得到鸭肝过氧化氢酶电泳纯制品，回收率为18．23％，比活达4780．38U／mg，纯化倍数为66．15。最适温度为40℃，最适pH为7．0，该酶在20～40℃，pH5～8内稳定．经凝胶过滤和SDS-PAGE测得该酶的全分子量为250KD，亚基分子量为62．5KD。

A catalase was purified from Anas platyrhynchos by homogenation, n-butanol disposal, ammonium sulfate precipitation, ion-exchange chromatography on DEAE-Sepharose Fast Flow column and gel filtration chromatography on Sephacryl S-200. The purity of the purified catalase was confirmed by the presence of a single band on SDS-PAGE. 18. 23% of the catalase activity was recovered. The specific activity was 4 780. 38 U/mg. The optimum pH and optimum temperature were 7.0 and 40 ℃, respectively. The catalase appeared to be stable at 20～40 ℃ and pH 5～8, and it was 66. 15-fold purified. Sephacryl S-200 chromatography and SDS-PAGE showed that the molecular weight of this catalase was 250 KD and its subunit was about 62. 5 KD.