链球菌产磷酸甘油氧化酶的基本特性  

Properties of L-α-glycerophosphate oxidase from Streptococcus SP.

作　　者：卢戌[1] 赵兴秀[1] 张锐[1] 孟尧[1] 武翠玲[1] 孟延发[1] 

机构地区：[1]四川大学生命科学学院生物资源与生态环境教育部重点实验室,成都610064

出　　处：《四川大学学报（自然科学版）》2006年第6期1379-1383,共5页Journal of Sichuan University(Natural Science Edition)

基　　金：国家科技部技术创新基金资助项目(04C26225120848)

摘　　要：介绍了经筛选的链球菌（StreptococcusSP．）产磷酸甘油氧化酶的分离纯化及部分性质的研究．发酵培养液经离心收集菌体，用超声波破碎，40％～75％硫酸铵沉淀法进行粗分级，再通过Q-Sepharose FF、Phenyl—Sepharose CL-4B、Chelating Sepharose FF和Sephacryl S-200HR层析纯化，纯化的磷酸甘油氧化酶在还原、非还原SDS-PAGE中显示单一条蛋白着色带并测得该酶的表观分子质量为67．6kDa，用HPLC测得其天然状态酶的表观分子质量为121kDa，据此推测该酶由两个分子质量相同的亚基组成．酶学动力学研究结果表明，该酶的最适温度为35℃，最适pH为8．0，最适条件下测得Km为3．22×10^-2mol／L．一些金属离子和某些有机物对酶活性的影响也进行了讨论．The L-a- glycerophosphate oxidase from Streptococcus SP. was purified by 40 % - 75 % ammonium sulfate precipitation, column chromatographies on Q-Sepharose FF, Phenyl-Sepharose CL-4B , Chelating Sepharose FF and Sephacryl S-200 HR. The purified L-a-glycerophosphate oxidase migrated as a single protein hand on reduced / non-reduced SDS-PAGE. The result showed that molecular weight of single peptide chain was 67.6 kDa. The native molecular weight of it was estimated to be about 121 kDa by HPLC. So the structure of L-a-glycerophosphate oxidase was consisted of two subunits with identical molecular weight. The optimum temperature and optimum pH for enzyme action were 3512 and pH 8.0 respectively. The Km of L- a-glycero-phosphate oxidase was 3.22× 10^-2mol/L at optimum conditions. Otherwise, some metal ions and some organic compounds on the enzyme activity were studied.

关 键 词：磷酸甘油氧化酶 STREPTOCOCCUS SP. 动力学特性 

分 类 号：Q554[生物学—生物化学]