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- W2074058514 abstract "The interaction between Phacolysin (PCL) and bovine serum albumin (BSA) under imitated physiological conditions was investigated by spectroscopic (fluorescence, UV-Vis absorption and Circular dichroism) techniques. The experiments were conducted at different temperatures (294K, 302K, 306K and 310K) and the results showed that the PCL caused the fluorescence quenching of BSA through a static quenching procedure. The binding constant (Ka), binding sites (n) were obtained. The corresponding thermodynamic parameters (ΔH, ΔS and ΔG) of the interaction system were calculated at different temperatures. The results revealed that the binding process was spontaneous and the acting force between PCL and BSA were mainly hydrogen bonding and van der Waals forces. According to Förster non-radiation energy transfer theory, the binding distance between PCL and BSA was calculated to be 2.41nm. What is more, both synchronous fluorescence and Circular dichroism spectra confirmed the interaction, which indicated the conformational changes of BSA." @default.
- W2074058514 created "2016-06-24" @default.
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- W2074058514 date "2014-06-01" @default.
- W2074058514 modified "2023-09-27" @default.
- W2074058514 title "Spectroscopic studies on the interaction of Phacolysin and bovine serum albumin" @default.
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- W2074058514 doi "https://doi.org/10.1016/j.saa.2014.02.064" @default.
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