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 ...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.展开更多
文摘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.
