| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 7631521 | Journal of Pharmaceutical and Biomedical Analysis | 2013 | 6 Pages |
Abstract
- Tolmetin interaction with human serum albumin (HSA) was analyzed by steady state and time resolved fluorescence spectroscopy.
- Results show ligand-HSA complex formation with 1:1 stoichiometry. The binding constants Ka was calculated for 25, 37 and 47 °C.
- The association process was exothermic (ÎH0Â <Â 0), predominantly enthalpy driven.
- Quenching efficiency calculations, based on steady-state and time-resolved fluorescence spectroscopy, indicate that both static and dynamic quenching mechanisms are present.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Silvia Neamtu, Nicoleta Tosa, Mircea Bogdan,