Thermal stability of porcine pepsin influenced by Al(III) ion: DSC study |
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Authors: | V M Pavelkić M V Beljanski K M Antić M M Babić T P Brdarić K R Gopčević |
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Institution: | 1.Institute “Kirilo Savi?”,Belgrade,Serbia;2.Institute of General and Physical Chemistry,Belgrade,Serbia;3.School of Medicine,University of Belgrade,Belgrade,Serbia |
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Abstract: | 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
L, 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
m), calorimetric (ΔH
cal) and van’t Hoff enthalpy (ΔH
VH), Gibbs free energy, Δ(ΔG), 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. |
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