Acid-induced denaturation and refolding of prothrombin

被引：10

作者：

Debnath, DK ^{[1
]}

Mukhopadhyay, K ^{[1
]}

Basak, S ^{[1
]}

机构：

[1] Saha Inst Nucl Phys, Div Chem Sci, Kolkata 700064, W Bengal, India

来源：

BIOPHYSICAL CHEMISTRY | 2005年 / 116卷 / 02期

关键词：

prothrombin; structural transitions; acid; partial unfolding; molten globule; ANS fluorescence; circular dichroism; light scattering;

D O I：

10.1016/j.bpc.2005.02.003

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：

Structural transitions of the blood coagulation factor prothrombin (extracted from goat blood) in response to reduction of pH were investigated by fluorescence, circular dichroism and light scattering measurements. The study revealed the presence of a partially unfolded state at around pH 3.5, characterized by marked enhancement of fluorescence from ANS bound to the protein, increase of bimolecular rate constant for tryptophan fluorescence quenching and a sharp peak in the light scattering intensity. Further lowering of the pH caused reversal of the trend of variation of these parameters, suggesting that prothrombin folds back to a compact state containing native-like secondary structural elements. The refolded state at low pH (< pH 3) fits the description of the A-state, the end-point of acid-induced denaturation process of several other monomeric proteins, and is a possible candidate for the class of folding intermediates known as molten globules. (c) 2005 Elsevier B.V. All rights reserved.

引用

页码：159 / 165

页数：7

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