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The binding reaction of oxymatrine (OMT) with bovine serum albumin (BSA) was studied by the methods of isothermal titration calorimetry, fluorescence, and circular dichroism (CD) spectroscopy. The thermodynamic results indicated that there were two classes of binding sites on the BSA molecule for OMT molecule. When the drug molecule binding to the first class of sites, the standard changes of enthalpy...
The interaction of matrine (MAT) with bovine serum albumin (BSA) was studied via applying isothermal titration calorimetry, fluorescence and circular dichroism spectra. Important thermodynamic parameters were obtained based on the assumption that there were several classes of binding sites on the biomacromolecules and the supposition that the binding of the drug with the protein could be represented...
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