Studies on cytochrome c-heparin interactions by differential scanning calorimetry.
The effects of heparin on the thermotropic properties of ferricytochrome c have been studied using high-sensitivity differential scanning calorimetry. Saturating concentrations of heparin at low ionic strength induced an important shift of the transition temperature Tm from 84.1 degrees C to 59.8 degrees C. This was accompanied by unusually large cooperativity of thermal denaturation of this complex, indicating strong intermolecular interactions between protein molecules. The destabilization of cytochrome c when mixed with heparin was not observed at high ionic strength, under which conditions complex was not formed.
Bágel'ová
J
J
Department of Biophysics, Slovak Academy of Science, Kosice.
Antalík
M
M
Bona
M
M
D002152:Calorimetry, Differential Scanning; D003574:Cytochrome c Group / Q000737:chemistry* / Q000378:metabolism*; D006493:Heparin / Q000378:metabolism*; D006358:Hot Temperature; D009994:Osmolar Concentration; D011489:Protein Denaturation; D012965:Sodium Chloride / Q000494:pharmacology; D013816:Thermodynamics
D003574:Cytochrome c Group; D012965:Sodium Chloride; D006493:Heparin