Effect of pH and Guanidine Hydrochloride on the Conformation of 57kDa Rat Liver Nuclear Thyroid Hormone Binding Protein Measured by Fluorescence
| Autor: | Mikiko Fujii, Nobuo Okabe |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Male
Thyroid Hormones Protein Conformation Hydrochloride Guanidines chemistry.chemical_compound Drug Discovery medicine Animals Denaturation (biochemistry) Thyroid hormone binding Guanidine Cell Nucleus Chemistry Binding protein Membrane Proteins Rats Inbred Strains General Chemistry General Medicine Hydrogen-Ion Concentration Fluorescence Rats Cell nucleus Spectrometry Fluorescence medicine.anatomical_structure Liver Biochemistry Rat liver Biophysics Triiodothyronine Carrier Proteins |
| Zdroj: | Chemical and Pharmaceutical Bulletin. 40:504-505 |
| ISSN: | 1347-5223 0009-2363 |
| DOI: | 10.1248/cpb.40.504 |
| Popis: | The denaturation of the 57 kilodalton (kDa) rat liver nuclear thyroid hormone binding protein (NTHB) by pH and guanidine hydrochloride (GdnHCl) has been investigated with the fluorescence method. The acid and alkaline fluorescence quenching suggests that the structure of NTHB is invariant in the relatively narrow pH region of approximately pH 7-9. A cooperative conformational transition occurred in GdnHCl concentrations of 1.5-2.5 m. The apparent free energy of unfolding of NTHB, delta G(appH2O) was evaluated as 6.31 (+/- 0.12) kcal.mol-1 at pH 7.7, 25 degrees C. |
| Databáze: | OpenAIRE |
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