Abstract：The interation of caffeine and theophylline with bovine serum albumins has been studied by fluorescence spectroscopy. The results indicated that enoxacin could bind with BSA strongly at molar ratio 1∶1 and the equilibrium constants were Kc=1.673×104 L·mol-1 and Kt=6.802×103 L·mol-1,respectively. Good linear Stern-Volmer lines were observed on the fluorescence of BSA quenched by enoxacin of different concentration, indicating that the combination reaction of enoxacin with BSA is a single static quenching process.
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