TY  - JOUR
AU  - Pavelkić, V.M.
AU  - Beljanski, M.V.
AU  - Antić, K.M.
AU  - Babić, Marija M.
AU  - Brdarić, T.P.
AU  - Gopčević, K.R.
PY  - 2011
UR  - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/6027
AB  - 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, KL, 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 (Tm), calorimetric (ΔHcal) and van’t Hoff enthalpy (ΔHVH), 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.
PB  - Pleiades Publishing
T2  - Russian Journal of Physical Chemistry A
T1  - Thermal stability of porcine pepsin influenced by Al(III) ion: DSC study
EP  - 2250
IS  - 13
SP  - 2245
VL  - 85
DO  - 10.1134/S003602441113022X
ER  - 

@article{
author = "Pavelkić, V.M. and Beljanski, M.V. and Antić, K.M. and Babić, Marija M. and Brdarić, T.P. and Gopčević, K.R.",
year = "2011",
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, KL, 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 (Tm), calorimetric (ΔHcal) and van’t Hoff enthalpy (ΔHVH), 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.",
publisher = "Pleiades Publishing",
journal = "Russian Journal of Physical Chemistry A",
title = "Thermal stability of porcine pepsin influenced by Al(III) ion: DSC study",
pages = "2250-2245",
number = "13",
volume = "85",
doi = "10.1134/S003602441113022X"
}

Pavelkić, V.M., Beljanski, M.V., Antić, K.M., Babić, M. M., Brdarić, T.P.,& Gopčević, K.R.. (2011). Thermal stability of porcine pepsin influenced by Al(III) ion: DSC study. in Russian Journal of Physical Chemistry A
Pleiades Publishing., 85(13), 2245-2250.
https://doi.org/10.1134/S003602441113022X

Pavelkić V, Beljanski M, Antić K, Babić MM, Brdarić T, Gopčević K. Thermal stability of porcine pepsin influenced by Al(III) ion: DSC study. in Russian Journal of Physical Chemistry A. 2011;85(13):2245-2250.
doi:10.1134/S003602441113022X .

Pavelkić, V.M., Beljanski, M.V., Antić, K.M., Babić, Marija M., Brdarić, T.P., Gopčević, K.R., "Thermal stability of porcine pepsin influenced by Al(III) ion: DSC study" in Russian Journal of Physical Chemistry A, 85, no. 13 (2011):2245-2250,
https://doi.org/10.1134/S003602441113022X . .