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- W2355720159 abstract "The interaction between Amido Black 10B(AB) and Bovine Serum Albumin(BSA) in aqueous solution was studied by UV-vis,fluorescence,and circular dichroism spectroscopy.The intrinsic fluorescence of BSA was quenched by Amido Black 10B,which was explained in terms of the ststics quenching mechanism.The number of binding sites and the apparent binding constants at different temperatures were obtained from Stern-volmer analysis of the fluorescence quenching date.The thermodynamic parameters determined by the Van't Hoff analysis of the binding constants(ΔH=-193.466 kJ,ΔS=-540.734 J·mol-1·K-1) clearly indicate that the hydrogen bond and Vander waals force are the main binding forces.Synchronous fluorescence spectroscopy and FT-IR spectra showed the conformation of BSA changed in the presence of AB." @default.
- W2355720159 created "2016-06-24" @default.
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- W2355720159 date "2011-01-01" @default.
- W2355720159 modified "2023-09-24" @default.
- W2355720159 title "Study on the interaction of Amido Black 10B and Bovine Serum Albumin by spectroscopic" @default.
- W2355720159 hasPublicationYear "2011" @default.
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