Laboratorio de Investigación Bioquímica, Programa Institucional en Biomedicina Molecular, Sección de Estudios de Posgrado, ENMyH-Instituto Politécnico Nacional, Guillermo Massieu Helguera No. 239, La Escalera Ticoman, DF, 07320, Mexico.
Protein J. 2010 Jan;29(1):1-10. doi: 10.1007/s10930-009-9215-y.
Enolase is a multifunctional protein that participates in glycolysis and gluconeogenesis and can act as a plasminogen receptor on the cell surface of several organisms, among other functions. Despite its participation in a variety of biological and pathophysiological processes, its stability and folding/unfolding reaction have not been fully explored. In this paper we present, the urea and GdnHCl-induced denaturation of enolase studied by means of fluorescence and circular dichroism spectroscopies. We found that enolase unfolds through a highly reversible pathway, populating a stable intermediate species in a range of experimental conditions. The refolding reaction also exhibits an intermediate state that might have a slightly more compact conformation compared to the unfolding intermediate. The thermodynamic parameters associated with the unfolding reaction are presented and discussed.
烯醇化酶是一种多功能蛋白，参与糖酵解和糖异生，并且可以作为几种生物体细胞表面的纤溶酶原受体等发挥作用。尽管它参与了多种生物和病理生理过程，但它的稳定性和折叠/展开反应尚未得到充分研究。在本文中，我们通过荧光和圆二色性光谱研究了脲和盐酸胍诱导的烯醇化酶变性。我们发现烯醇化酶通过一种高度可逆的途径展开，在一系列实验条件下形成稳定的中间态。复性反应也表现出一种中间状态，与展开中间态相比，可能具有稍微更紧凑的构象。本文还提出并讨论了与展开反应相关的热力学参数。
