作者: Xing-Jia Guo , Xiu-Dan Sun , Shu-Kun Xu
DOI: 10.1016/J.MOLSTRUC.2007.06.035
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摘要: Abstract The mutual interaction of riboflavin (RF) with bovine serum albumin (BSA) was investigated using fluorescence spectroscopy under simulative physiological conditions. quenching mechanism BSA by RF should belong to dynamic according the Stern–Volmer equation, but also effect ground complex formation and energy transfer could not be completely precluded in BSA–RF system. binding constants corresponding thermodynamic parameters at different temperatures were calculated, which indicated presence hydrophobic forces between BSA. averaged distance obtained based on theory FOrster’s non-radiation transfer. Moreover, conformation analyzed synchronous fluorescence. effects some common ions Cu 2+ , Zn Ca Mg constant examined.