A study of the interaction between fluorescein sodium salt and bovine serum albumin by steady-state fluorescence

被引:146
作者
Barbero, Nadia [3 ]
Barni, Ermanno [1 ,2 ]
Barolo, Claudia [1 ,2 ]
Quagliotto, Pierluigi [1 ,2 ]
Viscardi, Guido [1 ,2 ]
Napione, Lucia [3 ]
Pavan, Simona [3 ]
Bussolino, Federico [3 ]
机构
[1] Univ Turin, Dept Gen Chem & Organ Chem, I-10125 Turin, Italy
[2] Univ Turin, NIS, Interdept Ctr Excellence Q1, I-10125 Turin, Italy
[3] Univ Turin, Dept Oncol Sci, Inst Canc Res & Treatment, I-10060 Candiolo, TO, Italy
关键词
Bovine serum albumin; Fluorescein sodium salt; Spectroscopic studies; Binding studies; Steady-state fluorescence quenching; Association constants; Dissociation constants; BINDING; PROTEINS;
D O I
10.1016/j.dyepig.2008.08.006
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
The binding of fluorescein sodium Salt with three kinds of commercially available bovine serum albumin (BSA) of different grades Of purity Was investigated at 288, 298 and 313 K by fluorescence and absorption measurements at pH 7.50. The association and dissociation constants K-a and K-d were determined by the quenching of BSA fluorescence in the presence Of fluorescein sodium salt. The best results were obtained by fitting raw data by non-linear regression and Lineweaver-Burk equations. The modified Stern-Volmer and Scatchard plots gave less reliable data since the fitting was much more difficult. The agreement of the constants for the three sets of measurements conning from the different BSA was not as good as expected. BSA binding properties differ depending on the different BSA grades Of purity. Actually, the binding constants found for the three BSAs used differed ill the same set of interactions, even by keeping the experimental conditions constant. These results ire a novelty in the field of BSA-ligand binding studies and Should be taken into account for future binding Studies using BSA. Actually, a large number of aspects should be considered including the grade Of Purity and the presence of BSA covalent and non-covalent dimers, trimers and oligomers in Solution which call affect the goodness of the binding results. (C) 2008 Elsevier Ltd. All rights reserved.
引用
收藏
页码:307 / 313
页数:7
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