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家蚕表皮多酚氧化酶的分离纯化及酶学性质研究
引用本文:马晓春,韩宏岩,许维岸. 家蚕表皮多酚氧化酶的分离纯化及酶学性质研究[J]. 安徽农业科学, 2009, 37(17): 7870-7871
作者姓名:马晓春  韩宏岩  许维岸
作者单位:苏州大学基础医学与生物科学学院,江苏苏州,215123;苏州大学基础医学与生物科学学院,江苏苏州,215123;苏州大学基础医学与生物科学学院,江苏苏州,215123
摘    要:[目的]分离纯化家蚕多酚氧化酶,并对其性质进行分析研究。[方法]采用硫酸铵分级沉淀、凝胶过滤、蛋白质电泳等方法。[结果]多酚氧化酶分子量约为81kD;最适温度为30℃;最适pn值为7.0。低浓度金属离子Ag^+、Ca^2+、Mn^2+、Zn^2+对多酚氧化酶有一定的激活作用,而高浓度有抑制作用。[结论]金属离子对家蚕多酚氧化酶的影响很大,值得更深入的研究。

关 键 词:家蚕  多酚氧化酶  分离纯化  性质

Study on the Separation,Purification and Enzymatic Properties of Polyphenoloxidase from Epidermis of Bombyx mori
MA Xiao-chun et al. Study on the Separation,Purification and Enzymatic Properties of Polyphenoloxidase from Epidermis of Bombyx mori[J]. Journal of Anhui Agricultural Sciences, 2009, 37(17): 7870-7871
Authors:MA Xiao-chun et al
Affiliation:MA Xiao-chun et al (College of Preclinical Medicine , Biological Science,Soochow University,Suzhou,Jiangsu 215123)
Abstract:[Objective] The research aimed to separate and purify polyphenoloxidase from Bombyx mori and study its properties.[Method] The methods of ammonium sulfate precipitation,gel filtration,protein electrophoresis and so on were used.[Result] The molecular weight of polyphenoloxidase was about 81 kD.The optimum temperature was 30 ℃ and the optimum pH was 7.0.The metal ions of Ag+,Cu2+,Mn2+ and Zn2+ at low concentration had certain activation on polyphenoloxidase and that at high concentration had inhibition.[Conclusion] The influences of heavy metal ions on polyphenoloxidase from Bombyx mori were greater,to be worth further study.
Keywords:Bombyx mori  Polyphenoloxidase  Separation and purification  Properties  
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