菜豆多胺氧化酶的分离提纯及催化性质研究  

Purification of polyamine oxidase from Phaseolus vulgaris L. and its some kinetic parameters

作　　者：王明祖[1] 何生根[2] 杨暹[3] 

机构地区：[1]仲恺农业技术学院农业与园林学院,广东广州510225 [2]仲恺农业技术学院生命科学学院,广东广州510225 [3]华南农业大学园艺学院,广东广州510642

出　　处：《仲恺农业技术学院学报》2007年第1期9-12,共4页Journal of Zhongkai Agrotechnical College

基　　金：广东省自然科学基金(001425);广东省教育厅优秀人才培养基金(Q02041)资助项目

摘　　要：依次经粗提、丙酮沉淀和Sepharose Cl-4B柱层析等步骤对菜豆(Phaseolus vulgarisL.)多胺氧化酶进行了分离提纯.结果表明,纯化倍数为115.9,产率达43.90%.进一步分析该酶的部分催化性质表明,其最适底物为腐胺(Put),其次是尸胺(Cad);另外该酶对亚精胺(Spd)和精胺(Spm)也有一定的催化作用;该酶以Put和Cad为底物时的最适pH值均为7.0,以Spd和Spm为底物时的最适pH值为6.7.A polyamine oxidase （PAO） was purified 115.9-fold from embryonic buds of kidney bean （Phaseolus vulgaris L. ） seedlings by the successive steps involving crude extract, thrice acetone fractioations and Sepharose Cl-4B column chromatography, with high yield of PAO activity, which reached to 43.9%. The Km value of the enzyme is 0.46, 0.58, 1.59 and 3.78 mmoL/L respectively when the substrate is Put, Cad, Spd and Spm, thus diamines including Put and Cad are its effective substrates. The pH optimum of the enzyme was 7.0 when Put or Cad used as substrate, however, which was shifted to 6.7 when using Spd or Spm as substrate.

关 键 词：菜豆(Phaseolus VULGARIS L.) 多胺氧化酶 分离提纯 催化性质 

分 类 号：Q945[生物学—植物学]