期刊文献+

兼具SOD和GPX活力的双功能酶的制备及性质研究 被引量:2

Preparation and Properties of the Bifunctional Enzyme with both SOD and GPX Activities
下载PDF
导出
摘要 用苯甲基磺酰氟(PMSF)和H_2Se相继处理铜锌超氧化物岐化酶(Cu,Zn-SOD),将酶分子中的丝氨酸(Ser)转化为硒代半胱氨酸(SeCys),从而引入了谷胱甘肽过氧化物酶(GPX)的催化基团,使其在SOD酶活性大部分保留的情况下,具有GPX活性,其GPX活力是PZ51活力的30倍。研究了双功能酶的最佳制备条件,包括PMSF的剂量、反应最适温度及H_2Se处理时间等,并用电子能谱、DTNB等方法测定了双功能酶的硒含量;测定了双功能酶对不同底物的米氏常数及双功能酶的荧光光谱、紫外吸收光谱及稳定性。 The groups of Serinef(Ser)in superoxide dismutase(SOD) were selectively activated by phenylmethylsulfonyl fluoride (PMSF)and displaced with hydrogen selenide (H_2Se).Thus.Ser residues were mutated into selenocysteine (SeCys),which is the catalytic group of native glutathione peroxidase (GPX).Therefore,the mutated enzyme showed GPX activity and remained most of the original activity of native SOD. Its GPX activity was 30 times more than that of PZ 51. The optimal mutation conditions were established,such as PMSF concentration,reaction 52. temperature and time.The Se content of the mutated enzyme was determined by x-ray photoelectron spectrum and DTNB. Some properties of the mutated SOD,including kinetic data based on GPX activity,CD spectrum,storage stabilities etc. were also studied.
出处 《生物化学杂志》 CAS CSCD 1995年第6期673-678,共6页
基金 国家自然科学基金
关键词 超氧化物歧化酶 双功能酶 谷胱甘肽 过氧化物酶 Superoxide dismutase,Bifunctional enzyme,Glutathione peroxidase
  • 相关文献

同被引文献148

引证文献2

二级引证文献15

相关作者

内容加载中请稍等...

相关机构

内容加载中请稍等...

相关主题

内容加载中请稍等...

浏览历史

内容加载中请稍等...
;
使用帮助 返回顶部