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[尿素和磷酸根离子存在下β-乳球蛋白热变性的量热研究]

[Calorimetric study of the thermal denaturation of beta-lactoglobulin in the presence of urea and phosphate ions].

作者信息

Griko Iu V, Privalov P L

出版信息

Mol Biol (Mosk). 1992 Jan-Feb;26(1):150-7.

PMID:1508164
Abstract

The denaturation of beta-lactoglobulin in solution with different content of urea and phosphates has been studied calorimetrically. It has been shown that the increase of phosphate ion concentration in solution leads to an increase of beta-lactoglobulin stability, while increase of urea concentration leads to an opposite effect. The variation of these components in solution practically does not influence the value of the heat capacity increment of beta-lactoglobulin in the considered temperature region. Accordingly the denaturation enthalpy is a linear function of temperature whose slope does not differ for solution with urea concentration less than 4.4 M. However, the absolute value of denaturation enthalpy in these solutions at corresponding temperatures differs significantly due to the heat effect of additional urea solvation during transition to the denatured state. The latter leads to a decrease of the overall denaturation enthalpy and, as a result, a shift of the enthalpy plot to higher temperatures providing conditions for studying the thermodynamic and structural characteristics of the molecule in the cold denatured-state.

摘要

采用量热法研究了β-乳球蛋白在含有不同尿素和磷酸盐含量的溶液中的变性情况。结果表明,溶液中磷酸根离子浓度的增加会导致β-乳球蛋白稳定性的增加,而尿素浓度的增加则会产生相反的效果。溶液中这些成分的变化实际上不会影响所考虑温度范围内β-乳球蛋白的热容增量值。因此,变性焓是温度的线性函数,对于尿素浓度小于4.4 M的溶液,其斜率没有差异。然而,由于在转变为变性状态期间额外尿素溶剂化的热效应,这些溶液在相应温度下的变性焓绝对值存在显著差异。后者导致整体变性焓降低,结果使焓图向更高温度偏移,为研究分子在冷变性状态下的热力学和结构特征提供了条件。

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