摘要
运用双酶偶联体系分别测定6A,6A'-二苯胺-6B,6B'-二硒桥联-β-CD(6-AnSeCD)催化谷胱甘肽(GSH)还原过氧化氢(H2O2)、叔丁基过氧化氢(t-BuOOH)和枯烯过氧化氢(CumOOH)3种结构不同氢过氧化物的谷胱甘肽过氧化物酶(GPx)活力,并考察6-AnSeCD催化这3种氢过氧化物的稳态动力学.结果表明:6-AnSeCD还原CumOOH的GPx活力最高;6-AnSeCD的催化机制为乒乓机制;6-AnSeCD的假一级反应速度常数(k max)、米氏常数(K m)和二级反应速率常数(k)均显示CumOOH为6-AnSeCD的最适底物.
The gluathione peroxidase (GPx) activities of 6A, 6A'-dianilino-6B, 6B'-diselenide-bis β- cyclodextrin (6-AnSeCD) in the reduction of H202, tert-butyl hydroperoxide (t-BuOOH) and cumenyl hydroperoxide (CumOOH) by glutathione (GSH) were assessed in classical coupled reductase assay, and the steady-state kinetics of 6-AnSeCD in the reduction of three hydrogen peroxides was studied. The 6-AnSeCD displayed best GPx activity for the reduction of CumOOH by GSH. A ping-pong mechanism was observed in the steady-state kinetic studies on the 6-AnSeCD- catalyzed reactions. We further compared kmax, Km and second-order rate constant of 6-AnSeCD. The results show the CumOOH is the most preferred substrate for 6-AnSeCD.
出处
《吉林大学学报(理学版)》
CAS
CSCD
北大核心
2013年第5期961-964,共4页
Journal of Jilin University:Science Edition
基金
国家自然科学基金(批准号:21002040)
吉林大学科学前沿与交叉学科创新项目(批准号:200903093
2010ME005)