Studies on cytochrome c-heparin interactions by differential scanning calorimetry.

ABSTRACT: 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.

SUBMITTER: Bagel'ova J 

PROVIDER: S-EPMC1137796 | biostudies-other | 1994 Jan

REPOSITORIES: biostudies-other