鲐鱼消化道中蛋白酶的分离纯化及其活性研究  

Study on the isolation, purification and its properties of the protease from the alimentary canal of pneumatophorus japoni- cus

作　　者：于国英[1] 朱莉 韩志武[1] 杨选影[1] 

机构地区：[1]青岛大学医学院附属医院,山东青岛266003

出　　处：《中国海洋药物》2002年第4期54-56,共3页Chinese Journal of Marine Drugs

摘　　要：采用硫酸铵沉淀,DEAE-Sephadex A-50柱层析和Sephadex G-75凝胶过滤等方法,对鲐鱼消化道蛋白酶进行了分离纯化。实验证明,该酶既能水解酪蛋白,又能水解N-苯甲酞-L精氨酸乙酯（BAEE）。该酶水解酪蛋白的最适温度为50℃,最适pH为9.2×103mol·L-2Ca2+和Mg2+对该酶有激活作用,Hg2+,Co2+,Cu2+对该酶活性有抑制作用。2×10mol·L-1半胱氨酸、巯基乙醇、还原型谷胱甘肽对该酶活性无影响,碘乙酸和PCMB对该酶活性亦无影响,而2×10-3mol·L1EDTA则能明显地抑制其活性。By means of ammonium sulfate precipitation, DEAE-Sephadex A-50 chromatogra-phy and Sephadex G-75 get filtration, obtained a purificatory proteolytic enzyme from the alimentary canal of pneurnatophorus japonicus. The experiment had proved that the enzyme could not only hydrolyze casein but also hydrolyze BAEE. With casein as the substrate, the optimal temperature was 50℃ and the optimal pH was 92×10-1mol · L-1 Ca2+ and Mg2+ could activate the proteolytic activity of the enzyme, Hg2+ , Co2+ and Cu2+ could inhibit its activity. Neither cysteine, mercaptoethanol and glutathione (GHS) nor iodoacetic acid and PCMB could affect the activity of the enzyme. 2× 10-3mol·L-1 EDTA could obviously in-hibit the activity of the enzyme.

关 键 词：分离纯化 活性 鲭科鲐鱼 蛋白酶 

分 类 号：R282.77[医药卫生—中药学] R284[医药卫生—中医学]