A novel mimic was synthesized by modifying hyaluronic acid （HA） with tellurium, whose function is similar to that of glutathione peroxidase （GPX）. The structure of TeHA was characterized by means of IR and NMR, th...A novel mimic was synthesized by modifying hyaluronic acid （HA） with tellurium, whose function is similar to that of glutathione peroxidase （GPX）. The structure of TeHA was characterized by means of IR and NMR, the target-Te was located at -CH2OH of the N-acetyl-D- glucosamine of HA. The H202 reducing activity of TeHA, by glutathione （GSH）, was 163.6 U/μmol according to Wilson＇s method. In contrast to other mimics, TeHA displayed the highest activity. Moreover, TeHA accepted many hydroperoxides as its substrates, such as H2O2, cumenyl hydroperoxide （CuOOH） and tert-butyl hydroperoxide （t-BuOOH）, and CuOOH was the optimal substrate of TeHA. A ping-pong mechanism was observed in the steady-state kinetic studies of the reactions catalyzed by TeHA.展开更多
文摘A novel mimic was synthesized by modifying hyaluronic acid （HA） with tellurium, whose function is similar to that of glutathione peroxidase （GPX）. The structure of TeHA was characterized by means of IR and NMR, the target-Te was located at -CH2OH of the N-acetyl-D- glucosamine of HA. The H202 reducing activity of TeHA, by glutathione （GSH）, was 163.6 U/μmol according to Wilson＇s method. In contrast to other mimics, TeHA displayed the highest activity. Moreover, TeHA accepted many hydroperoxides as its substrates, such as H2O2, cumenyl hydroperoxide （CuOOH） and tert-butyl hydroperoxide （t-BuOOH）, and CuOOH was the optimal substrate of TeHA. A ping-pong mechanism was observed in the steady-state kinetic studies of the reactions catalyzed by TeHA.
