| Autor: |
Pavelkić, V., Beljanski, M., Antić, K., Babić, M., Brdarić, T., Gopčević, K. |
| Zdroj: |
Russian Journal of Physical Chemistry; Dec2011, Vol. 85 Issue 13, p2245-2250, 6p |
| Abstrakt: |
Differential scanning calorimetry (DCS) has been used to determine thermodynamic profile of pepsin and the in vitro effect of Al(III) ions. Thermograms of pepsin unfolding in the presence and absence of aluminum were used to determine the binding constant, K, in the pepsin-aluminium model system. The thermodynamic parameters were derived from DSC profiles at different ligand concentrations (1, 5 and 10 mM). The temperatures of thermal transitions ( T), calorimetric (Δ H) and van't Hoff enthalpy (Δ H), Gibbs free energy, Δ(Δ G), of Al(III) binding to pepsin, as well as an average number of ligands bound to the native protein, were obtained from DSC profiles too. Temperature-dependent changes in the protein structure were also monitored by native PAGE electrophoresis. Increasing the temperature causes the decrease in electrophoretic mobility. Increase in concentration of Al(III) decelerate the migration of pepsin samples on concentration dependent manner. Analysis showed that ligand binding increases thermal stability of protein. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
|
Full text from SpringerLink