Author(s): Hu YJ, Liu Y, Wang JB, Xiao XH, Qu SS
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Abstract The interaction between monoammonium glycyrrhizinate (MAG) and bovine serum albumin (BSA) were studied by fluorescence and absorption spectroscopy. The quenching mechanism of fluorescence of bovine serum albumin by monoammonium glycyrrhizinate was discussed. The binding sites number n and apparent binding constant K were measured by fluorescence quenching method. The thermodynamic parameters DeltaH degrees , DeltaG degrees , DeltaS degrees at different temperatures were calculated. The distance r between donor (bovine serum albumin) and acceptor (monoammonium glycyrrhizinate) was obtained according to Forster theory of non-radiation energy transfer. The results of synchronous fluorescence spectra and UV-vis absorption spectra show that the conformation of bovine serum albumin has been changed.
This article was published in J Pharm Biomed Anal
and referenced in Journal of Molecular and Genetic Medicine