Binding of Methyl Pheophorbide-a-Gd to Bovine Serum Albumins
来源期刊：Journal of Rare Earths2006年第S2期
论文作者：李改枝 李桂芝
文章页码：332 - 335
摘 要：The binding reaction between methyl pheophorbide-a-Gd （MPA-Gd） and bovine serum albumins （BSA） were studied by fluorescence quenching technique and UV-Vis absorption spectra. The quenching mechanism of fluorescence of BSA by MPA-Gd was discussed. The binding equilibrium constant K0=4.4916×104 L·mol-1 at 25 ℃. The distance r between donor （BSA） and acceptor （MPA-Gd） was obtained according to Frster′s nonradiative energy transfer. The thermodynamic parameters ΔH, ΔG and ΔS were calculated at 25 and 37 ℃. The results indicate that the hydrophobic force played major role in the reaction. Furthermore, the displacement experiments indicate that MPA-Gd could bind to the site I of BSA.
李改枝，李桂芝
摘 要：The binding reaction between methyl pheophorbide-a-Gd （MPA-Gd） and bovine serum albumins （BSA） were studied by fluorescence quenching technique and UV-Vis absorption spectra. The quenching mechanism of fluorescence of BSA by MPA-Gd was discussed. The binding equilibrium constant K0=4.4916×104 L·mol-1 at 25 ℃. The distance r between donor （BSA） and acceptor （MPA-Gd） was obtained according to Frster′s nonradiative energy transfer. The thermodynamic parameters ΔH, ΔG and ΔS were calculated at 25 and 37 ℃. The results indicate that the hydrophobic force played major role in the reaction. Furthermore, the displacement experiments indicate that MPA-Gd could bind to the site I of BSA.
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