Study on the Features of the Binding Reaction Between Pefloxacin and Bovine Serum Albumin Using Fluorescence Spectrophotometry

摘要: Abstract Under different temperatures, the binding of pefloxacin to bovine serum albumin (BSA) was studied by means fluorescence quenching spectrum, synchronous three-dimensional and ultra-violet spectrum. After analyzing data using Stern-Volmer equation, Lineweaver-Burk equation thermodynamic average value bonding constant (KLB: 8.419 × 103 M), parameters (ΔHθ:150.7 KJ mol−1, ΔGθ:−22.88 ΔSθθ:561.9 J K−1), number sites (1.081) were obtained. It has been proved that BSA can react with each other form a new compound under experimental concentrations being static force hydrophobic force. provides important information for studying pharmacological effects biological configuration changes caused in proteins.