Studies on cytochrome c-heparin interactions by differential scanning calorimetry.
作者信息
Bágel'ová J, Antalík M, Bona M
机构信息
Department of Biophysics, Slovak Academy of Science, Kosice.
出版信息
Biochem J. 1994 Jan 1;297 ( Pt 1)(Pt 1):99-101. doi: 10.1042/bj2970099.
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.
摘要
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