萝卜中具溶菌酶活性组分的分子结构分析  

Research on the Molecular Structures of Chitin-binding Proteins with Lysozyme Activity from Raphanus sativus

作　　者：赖晓芳[1] 沈善瑞[1] 王炜军[2] 徐凤彩[2] 

机构地区：[1]淮海工学院海洋学院,江苏连云港222005 [2]华南农业大学生命科学学院,广东广州510642

出　　处：《安徽农业科学》2012年第27期13267-13269,共3页Journal of Anhui Agricultural Sciences

基　　金：江苏省海洋生物技术重点建设实验室开放基金(2008HS019);淮海工学院博士启动基金(KQ11010);淮海工学院自然科学基金(KX11111)

摘　　要：[目的]分析萝卜具有溶菌酶活性组分CBPs的分子结构,以期为其作用机制和在萝卜中的生理功能提供资料。[方法]利用亲和层析法及CM-纤维素离子交换柱层析分离纯化CBPs,测定其氨基酸组成、糖基和溶菌酶活性中心残基。[结果]从萝卜中得到了2个具溶菌酶活性且无糖基的组分:CBP1和CBP2,它们间氨基酸组成差异不大;Asp/Glu和His专一性化学修饰剂单独作用后,CBP1和CBP2相对溶菌酶活力均大幅度降低,预先加入竞争性抑制剂则下降的幅度减小。[结论]萝卜中有2个具溶菌酶活性的非糖蛋白组分,其溶菌酶活性中心氨基酸残基均可能含有Asp/Glu和His。[Objective] To analyze the molecular structure of chitin-binding proteins（CBPs） with lysozyme activity,so as to provide the material for understanding the catalysis mechanism and physiology function of CBPs.[Method] CBPs were purified by affinity chromatography and cation exchange chromatography on a CM-cellulose column,and then the amino acid components,glycoprotein,and the active center of lysozyme activity were determined.[Result] There were two purified fractions from Raphanus sativus with lysozyme activity： CBP1 and CBP2,which were not glycoprotein.After modified by special modification agents,the lysozyme activity was inhibited notably,which could be pre-protected by GlcNAc.[Conclusion] It could be estimated that Asp/Glu and His were the catalytic center of CBP1 and CBP2 lysozyme activity.

关 键 词：萝卜 溶菌酶活性 分子结构 

分 类 号：S631.1[农业科学—蔬菜学] Q522.2[农业科学—园艺学]