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.
出处
《化学研究与应用》
CAS
CSCD
北大核心
2006年第12期1408-1412,共5页
Chemical Research and Application
关键词
喜树碱
胰蛋白酶
紫外光谱
荧光淬灭
camptothecin
trypsin
ultraviolet spectrum
fluorescen quenching
