Kale K, Kresheck G C, Vanderkooi G
Biochim Biophys Acta. 1978 Aug 21;535(2):334-41. doi: 10.1016/0005-2795(78)90099-5.
The interactions of sodium dodecyl sulfate with cytochrome c and erythrocyte glycoproteins have been studied by the method of titration calorimetry. It was found that the initial addition of sodium dodecyl sulfate to cytochrome c caused an endothermic unfolding of the protein, detectable by circular dichroism (CD). This was followed by the exothermic binding of sodium dodecyl sulfate to the protein, without further CD-detectable conformational changes. In contrast, sodium dodecyl sulfate bound directly to the erythrocyte glycoproteins in an exothermic reaction without any accompanying CD-detectable conformation changes. This indicates that the glycoproteins solubilized in aqueous media have exposed hydrophobic regions which can interact directly with this detergent. The enthalpy changes and stoichiometries of binding are reported.
通过滴定热分析法研究了十二烷基硫酸钠与细胞色素c和红细胞糖蛋白的相互作用。发现最初向细胞色素c中添加十二烷基硫酸钠会导致蛋白质发生吸热去折叠，这可通过圆二色性（CD）检测到。随后是十二烷基硫酸钠与蛋白质的放热结合，且没有进一步可通过CD检测到的构象变化。相比之下，十二烷基硫酸钠以放热反应直接与红细胞糖蛋白结合，没有任何伴随的可通过CD检测到的构象变化。这表明溶解在水性介质中的糖蛋白具有可直接与这种去污剂相互作用的暴露疏水区域。报道了结合的焓变和化学计量。
