家蚕铜锌超氧化物歧化酶的分离纯化及其部分性质的研究  

Isolation,Purification and Some Properties of Copper/Zine Superoxide Dismutase in Silkworm

作　　者：唐云明[1] 鲁成[1] 向仲怀[1] 

机构地区：[1]农业部蚕桑学重点开放实验室

出　　处：《蚕业科学》2001年第2期96-99,共4页ACTA SERICOLOGICA SINICA

基　　金：国家自然科学基金重点项目! (39730 370 );重庆市科委资助课题

摘　　要：家蚕体液经热变性、DEAE 琼脂糖柱层析、SephacrylS 2 0 0凝胶过滤和等电点聚焦电泳纯化 ,获得达到均一程度的高活性的铜锌超氧化物歧化酶 (Cu .Zn SOD)。活性回收率为 35 % ,纯化倍数为 1911倍。测得该酶的分子量约为 32 0 0 0D ,亚基分子量约为 16 0 0 0D。该酶在紫外光区与可见光区的吸收峰分别为 2 70nm和 6 76nm。测得该酶的等电点为pH 7.15。High active Copper Zine and superoxide dismutase Cu.Zn SOD from silkworm body fluid has been isolatedand purified by denaturization with heating,DEAD sepharose column chromatography,Sephacryl S 200 gel filtration and isoelectric focusing electrophoresis.35% of the Cu.Zn SOD activity was recovered.Cu.Zn SOD was 1911 fold purified.The molecular weight of the purified Cu.Zn SOD is about 32,000 daltons as measured by Sephacryl S 200 gel filtration ,that of Cu.Zn SOD subunit is about 16,000 daltons as assayed by sodium dodecyl sulphate polyacrylamide gel electrophoresis.The enzyme exhibits two absorption maximum at 270nm ultraviolet and at 676nm visible region respectively.Isoelectric point of the enzyme was pH 7.15.

关 键 词：家蚕 铜锌超氧化物歧化酶 分离 纯化 基因 酶学性质 

分 类 号：S881[农业科学—特种经济动物饲养]