Journal of Thermal Analysis and Calorimetry

, Volume 82, Issue 1, pp 281–285 | Cite as

The effect of pH ont he thermal stability of<span style='font-size:10.0pt;font-family:"SymbolProp BT";mso-bidi-font-family:"SymbolProp BT"'>a-actin isoforms

  • G. Papp
  • Beáta Bugyi
  • Z. Ujfalusi
  • Sz. Halasi
  • J. Orbán

Summary

The effect of pH was characterised on the thermal stability of magnesium saturated skeletal and cardiac α-actin isoforms with differential scanning calorimetry (DSC) at pH 7.0 and 8.0. The calorimetric curves were further analysed to calculate the enthalpy and transition entropy changes. The activation energy was also determined to describe the energy consumption of the initiation of the thermal denaturation process. Although the difference in Tmvalues is too small to interpret the difference between the a-actin isoforms, the values of the activation energy indicated that the α-skeletal actin is probably more stable compared to the α-cardiac actin. The difference in the activation energies indicated that lowering the pH can produce a more stable protein matrix in both cases of the isoforms. The larger range of the difference in the values of the activation energies suggested that the α-cardiac actin is probably more sensitive to the change of the pH compared to the α -skeletal actin.

calorimetry activation energy pH actin isoform divalent cation 

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Copyright information

© Springer-Verlag/Akadémiai Kiadó 2005

Authors and Affiliations

  • G. Papp
    • 1
  • Beáta Bugyi
    • 2
  • Z. Ujfalusi
    • 3
  • Sz. Halasi
    • 4
  • J. Orbán
    • 5
  1. 1.University of Pécs, Faculty of Medicine, Department of Byophysics
  2. 2.University of Pécs, Faculty of Medicine, Department of Biophysics
  3. 3.Research Group for Fluoresence Spectroscopy, Office for Academy Research Groups Attached to Universities
  4. 4.University of Pécs, Faculty of Medicine, Department of Byophysics
  5. 5.University of Pécs, Faculty of Medicine, Department of Byophysics,

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