At different temperatures,the interaction feature of hesperidin and bovine serum albumin(BSA) was studied by fluorescence quenching spectra,three-dimensional fluorescence spectra and synchronous fluorescence spectra.It was proved that only dynamic quenching exits between hesperidin and BSA.Quenching constant is obtained at different temperatures.The binding site is a distance 3.29 nm away from tryptophan residue-212 in BSA based on Frster′s non-radiation energy transfer mechanism.According to the thermodyn...
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