Discrete reduction of type I collagen thermal stability upon oxidation

被引:58
作者
Komsa-Penkova, R
Koynova, R
Kostov, G
Tenchov, B [1 ]
机构
[1] Bulgarian Acad Sci, Inst Biophys, BU-1113 Sofia, Bulgaria
[2] Med Univ Pleven, Dept Biochem, Pleven 5802, Bulgaria
关键词
oxidation; collagen type I; thermal denaturation; Fe ions; thermal stability; specific volume (DSC);
D O I
10.1016/S0301-4622(99)00135-0
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 oxidation of acid-soluble calf skin collagen type I caused by metal-dependent free radical generating systems, Fe(II)/H2O2 and Cu(II)/H2O2, was found to bring down in a specific, discrete way the collagen thermal stability, as determined by microcalorimetry and scanning densitometry. Initial oxidation results in splitting of the collagen denaturational transition into two components. Along with the endotherm at 41 degrees C typical for non-oxidized collagen, a second, similarly cooperative endotherm appears at 35 degrees C and increases in enthalpy with the oxidant concentration and exposure time, while the first peak correspondingly decreases. The two transitions at 35 and 41 degrees C were registered by densitometry as stepwise increases of the collagen-specific volume. Further oxidation results in massive collagen destruction manifested as abolishment of both denaturational transitions. The two oxidative systems used produce identical effects on the collagen stability but at higher concentrations of Cu(II) in comparison to Fe(II). The discrete reduction of the protein thermal stability is accompanied by a decrease of the Gee amino groups, suggestive of an oxidation attack of the side chains of lysine residues. Since the denaturation temperature of collagen shifts from above to below body temperature (41 degrees C-35 degrees C) upon oxidation, it appears important to account for this effect in a context of the possible physiological implications of collagen oxidation. (C) 1999 Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:185 / 195
页数:11
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