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The binding equilibrium between phosphotungstic acid (H7[P(W2O7)6] · XH2O;PTA) and human serum albumin (HSA) or bovine serum albumin (BSA) has been studied by UV-Vis, fluorescence spectroscopies and equilibrium dialysis. It has been observed that UV absorption enhanced and the fluorescence quenched as the PTA binding to HSA or BSA at physiological pH 7.43(?.02). The Scatchard analysis indicated that there exists a strong binding site of PTA in both HSA and BSA, and the successive stability constants of these two systems are obtained by nonlinear least-squares methods fitting Bjerrum formula.
The binding equilibrium between phosphotungstic acid (H7 [P (W2O7) 6] XH2O; PTA) and human serum albumin (HSA) or bovine serum albumin (BSA) has been studied by UV- Vis, fluorescence spectroscopies and equilibrium dialysis has observed that UV absorption enhanced and the fluorescence quenched as the PTA binding to HSA or BSA at physiological pH 7.43 (?. 02). The Scatchard analysis indicated that there exists a strong binding site of PTA in both HSA and BSA, and the successive stability constants of these two systems are obtained by the nonlinear least-squares methods fitting Bjerrum formula.