【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。更多还原

【Abstract】 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 the latter,enhances UV absorption of pancreatic amylase,and results in a static quenching of theophylline to pancreatic amylase.更多还原