Effect of guanidine hydrochloride on bovine serum albumin complex with antithyroid drugs: fluorescence study
| Autor: | Anna Sułkowska, J Poźycka, Wiesław W. Sułkowski, Barbara Bojko, J. Równicka, I. Zubik-Skupień |
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| Rok vydání: | 2004 |
| Předmět: |
Chromatography
Quenching (fluorescence) biology Hydrochloride Organic Chemistry Albumin Uracil Binding constant Analytical Chemistry Inorganic Chemistry chemistry.chemical_compound chemistry biology.protein heterocyclic compounds Denaturation (biochemistry) Bovine serum albumin Guanidine Spectroscopy Nuclear chemistry |
| Zdroj: | Journal of Molecular Structure. 704:291-295 |
| ISSN: | 0022-2860 |
| DOI: | 10.1016/j.molstruc.2003.12.065 |
| Popis: | Denaturation of bovine serum albumin (BSA) with guanidine hydrochloride (Gu·HCl) was studied in the presence of mercaptopyrimidine (MPI) and uracil. With increasing unfolding of albumin due to Gu·HCl presence, the displacement of both MPI and model compound - uracil occurs. The spectroscopic analysis suggests that uracil and MPI binding sites are close to or located in the IB or IIA subdomains. Binding of both uracil and MPI to unfolded BSA is observed. The antidenaturant properties of uracil are shown. The binding and quenching constants were calculated for the uracil-BSA complex and in the presence of the denaturant (Gu·HCl). Structural changes due to 1.7 M Gu HCl led to the lowering of the binding constant by ∼14%. These changes rise with unfolding BSA. |
| Databáze: | OpenAIRE |
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