Thermal stability of porcine pepsin influenced by Al(III) ion: DSC study
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2011
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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 b...inding increases thermal stability of protein.
Ključne reči:
Activity / Differential scanning calorimetry / Ligand binding / PAGE electrophoresis / Pepsin / Thermal unfoldingIzvor:
Russian Journal of Physical Chemistry A, 2011, 85, 13, 2245-2250Izdavač:
- Pleiades Publishing
Finansiranje / projekti:
- Fizička hemija dinamičkih stanja i struktura neravnotežnih sistema - od monotone do oscilatorne evolucije i haosa (RS-MESTD-MPN2006-2010-142025)
- Dinamika nelinearnih fizičkohemijskih i biohemijskih sistema sa modeliranjem i predviđanjem njihovih ponašanja pod neravnotežnim uslovima (RS-MESTD-Basic Research (BR or ON)-172015)
DOI: 10.1134/S003602441113022X
ISSN: 0036-0244
WoS: 000297922700001
Scopus: 2-s2.0-85050303964
Institucija/grupa
Tehnološko-metalurški fakultetTY - 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 . .