Abstract
ABSTRACT The interaction between bovine serum albumin and ligustrazine was studied by fluorescence spectroscopy, synchronous fluorescence spectroscopy, UV-visible absorption spectroscopy, and circular dichroism spectroscopy. The results indicated that the hydrophobic force was the dominant intermolecular force in stabilizing the complex, and the probable quenching mechanism of the bovine serum albumin–ligustrazine interaction was initiated by complex formation. Also, the reaction was determined to be spontaneous. The effect of ligustrazine on the conformation of bovine serum albumin was analyzed using synchronous fluorescence and circular dichroism. The effects of seven metal ions on the binding properties of ligustrazine with bovine serum albumin were discussed.
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