Binding equilibrium study of phosphotungstic acid and HSA or BSA with UV spectrum, fluorescence spectrum and equilibrium dialysis  

作　　者：黄瑾 袁余洲 梁宏 

出　　处：《Science China Chemistry》2002年第2期200-207,共8页中国科学（化学英文版）

基　　金：This work was supported by the National Natural Science Foundation of China (Grant No.29961001); the Cross-Century Talents Foundation of Guangxi Zhuang Autonomous Region and Science Foundation of Guangxi University.

摘　　要：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( ± 0.02). 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. 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(±0.02). 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.

关 键 词：serum albumin  phosphotungstic acid  UV spectrum  fluorescence spectrum  equilibrium dialysis. 

分 类 号：O657.3[理学—分析化学]