STUDIES ON CYTOCHROME-C HEPARIN INTERACTIONS BY DIFFERENTIAL SCANNING CALORIMETRY

被引：35

作者：

BAGELOVA, J

ANTALIK, M

BONA, M

机构：

[1] Department of Biophysics, Institute of Experimental Physics, Slovak Academy of Sciences

来源：

BIOCHEMICAL JOURNAL | 1994年 / 297卷

关键词：

D O I：

10.1042/bj2970099

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 T-m 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.

引用

页码：99 / 101

页数：3

共 18 条

[11] MEMBRANE-BINDING INDUCES DESTABILIZATION OF CYTOCHROME-C STRUCTURE [J].