摘要
考察茶碱对胰α-淀粉酶的抑制作用,并通过紫外光谱法和荧光光谱法研究茶碱与胰α-淀粉酶的结合方式。以1/v对抑制剂量用Dixon作图法得出Ki值为0.59×10-2mol/L,抑制剂类型为非竞争性抑制。茶碱镶嵌于胰α-淀粉酶分子之间,形成了特定结构的缔合物,从而改变后者分子构象,使胰α-淀粉酶的紫外吸收差谱迅速增强,特征荧光峰产生静态淬灭。
In addition to studying the linking pattern between theophylline and pancreatic amylase by using ultraviolet and fluorescent spectrometry,the inhibition of theophylline over pancreatic amylase was also investigated in this research.Ki (0.59×10-2 mol/L) was educed by Dixon graphical chart with 1/v versus amount of inhibitor.The result shows that inhibitor is a noncompetitive one.The bondage between theophylline and pancreatic amylase forms a stable complex compound,which alters the molecular configuration of...
出处
《天然产物研究与开发》
CAS
CSCD
2008年第2期298-301,共4页
Natural Product Research and Development
关键词
茶碱
胰α-淀粉酶
紫外光谱
荧光光谱
theophylline
pancreatic amylase
prohibitive function
ultraviolet spectra
fluorescent spectra