摘要
采用超声波破碎、硫酸铵分级沉淀、Sephadex G-100和DE-52柱层析，从橄榄中分离纯化Cu，Zn—SOD，并对其部分性质进行分析鉴定。结果得到酶的比活力为906．3U／mg。该酶对Hzoz和KCN敏感，而T氏液对酶活性没影响。紫外吸收峰在275nm处，PAGE蛋白和活性染色呈现3条相对应的谱带，相对分子质量约为31．63kD，亚基相对分子质量约为15．73kD。此酶对热稳定，在pH7～9范围内稳定。
Copper-zinc superoxide dismutase was purified from Canarium album by ultrasonic, precipitation with ammoniurn sulfate,Sephadex G-100 filtration and DE-52 chromatography. And its characters were analyzed. The results showed that the specific activity of the enzyme was 906.3 U/mg. The enzyme activity was inhibited by KCN and H202, but it was not affected by Tsuchihashi solution. Its ultraviolet absorption peak was at 275 nm. Three protein bands of the enzyme correspond with its activity bands by polyacrylamide gel electrophoresis. Its relative molecular quality was 31.63 kD and subunit relative molecular quality was 15.73 kD. The enzyme had good heat stability and acid-base stability in pH7.0～9.0.
出处
《天然产物研究与开发》
CAS
CSCD
2007年第2期198-201,共4页
Natural Product Research and Development
关键词
橄榄
超氧化物歧化酶
分离纯化
Canarium album
superoxide dismutase
purification
