摘要
以羊血为原料,通过热处理、透析、离子交换层析等方法获得SOD提取物,测定其酶活力和蛋白质含量,并从温度、pH稳定性和外源试剂耐受性等几个方面对SOD稳定性进行了研究.结果表明:经过离子交换层析后,SOD的比活力达到5289.1U·mg-1,回收率为60%,纯化倍数为25.3倍;在40～60℃保温30min,SOD酶活力基本不变;pH6～9范围内SOD的稳定性较好;SOD对2mmol·L-1H2O2和尿素较敏感,2mmol·L-1SDS对SOD没有明显的抑制作用.
Enzyme activity and protein content of superoxide dismutase（SOD）extracted from sheep blood through hematolysis,precipitation and ion-exchange chromatography were determined,and the effects of temperature,pH and external reagent tolerance on stability of SOD were also studied.The results showed that the relative activity,yield ratio and purification times of SOD extracted from sheep blood were up to 5 289.1U·mg^-1,60% and 25.3 times respectively.The enzyme could keep better stability at the pH range from 6 to 9 and thermal stability at 40℃ to 60℃ for 30 mimutes.The SOD was sensitive to 2mmol·L^-1 H2O2,but not obviously inhibited by 2mmol·L^-1 SDS.
出处
《甘肃农业大学学报》
CAS
CSCD
北大核心
2010年第5期157-160,共4页
Journal of Gansu Agricultural University
基金
甘肃省农业生物技术研究与应用开发项目(GNSW-2010-03)
关键词
羊血
SOD
离子交换层析
稳定性
sheep blood
SOD
ion-exchange chromatography
stability
