喜树碱与胰蛋白酶的相互作用  

Interaction between Trypsin and Camptothecin

作　　者：贾旭[1] 邓珊珊[2] 李政[1] 苏波[1] 刁家志[1] 刘芯韵[1] 郑芸[1] 刘克武[1] 

机构地区：[1]四川大学生命科学学院生物资源与生态环境教育部重点实验室,四川成都610064 [2]江南大学生物工程学院,江苏无锡214036

出　　处：《化学研究与应用》2006年第12期1408-1412,共5页Chemical Research and Application

摘　　要：The interaction of trypsin with camptothecin(CPT) in vitro was studied by ultraviolet(UV) absorption spectral and fluorescence spectral methods.Making out value of Ki according to the ratio between 1/v and the amount of inhibitor contributes to the conclusion that CPT is a noncompetitive inhibitor.The interaction between CPT and trypsin is quite strong.CPT can affect the conformation of trypsin in some degree.Fluorescence quenching contributes to nonradiative energy-transfer,which results a static quenching of CPT to trypsin.Their binding constants and the binding sites of CPT were determined.The interaction of trypsin with camptothecin（CPT） in vitro was studied by ultraviolet （UV） absorption spectral and fluorescence spectral methods. Making out value of Ki according to the ratio between 1/v and the amount of inhibitor contributes to the conclusion that CPT is a noncompetitive inhibitor. The interaction between CPT and trypsin is quite strong. CPT can affect the conformation of trypsin in some degree. Fluorescence quenching contributes to nonradiative energy-transfer, which results a static quenching of CPT to trypsin. Their binding constants and the binding sites of CPT were determined.

关 键 词：喜树碱 胰蛋白酶 紫外光谱 荧光淬灭 

分 类 号：O629.3[理学—有机化学]