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The interaction between clarithromycin (CAM) and bovine serum albumin (BSA) was investigated using linear-sweep voltammetry in pH 7.4 phosphate buffer solution where CAM caused two irreversible reduction waves P2 and P3 on mercury electrode. The study showed that the formation constant and formation ratio for the interaction between CAM and BSA were 1.51×1012 and 3:1 for P2,4.53×105 and 1:1 for P3, respectively. The ion strength enhanced the hydrophobic interaction between CAM and BSA.
The interaction between clarithromycin (CAM) and bovine serum albumin (BSA) was investigated using linear-sweep voltammetry in pH 7.4 phosphate buffer solution where CAM caused two irreversible reduction waves P2 and P3 on mercury electrode. The study showed that the formation constant and formation ratio for the interaction between CAM and BSA were 1.51 × 1012 and 3: 1 for P2, 4.53 × 105 and 1: 1 for P3, respectively. The ion strength enhanced hydrophobic interaction between CAM and BSA.