Studies of the Interaction between Isoimperatorin and Human Serum Albumin by Multispectroscopic Method: Identification of Possible Binding Site of the Compound Using Esterase Activity of the Protein

<table>The Stern-Volmer plots for HSA fluorescence quenching by isoimperatorin at 298 (<i>◆</i>), 303 (▲), 308 (■), and 313 (●) K. The final protein concentration in 50 mM phosphate, pH 7.5, was 3 <i>μ</i>M. Based on “One-Sample Kolmogorov-Smirnov Test,” test distribution was normal.</table>

The Scientific World Journal

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Figure 4

Figure 4: Studies of the Interaction between Isoimperatorin and Human Serum Albumin by Multispectroscopic Method: Identification of Possible Binding Site of the Compound Using Esterase Activity of the Protein 

Figure 4 | Studies of the Interaction between Isoimperatorin and Human Serum Albumin by Multispectroscopic Method: Identification of Possible Binding Site of the Compound Using Esterase Activity of the Protein 