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用差示扫描量热法研究细胞色素c与肝素的相互作用

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.

DOI:10.1042/bj2970099
PMID:8280115
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1137796/
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

已使用高灵敏度差示扫描量热法研究了肝素对高铁细胞色素c热致性质的影响。在低离子强度下，饱和浓度的肝素会使转变温度Tm发生显著偏移，从84.1℃降至59.8℃。这伴随着该复合物热变性的异常大的协同性，表明蛋白质分子之间存在强烈的分子间相互作用。在高离子强度下未观察到细胞色素c与肝素混合时的稳定性降低，在这种条件下不会形成复合物。

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Domains in the fibrinogen molecule.纤维蛋白原分子中的结构域。
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