Bina M, Sturtevant J M, Stein A
Proc Natl Acad Sci U S A. 1980 Jul;77(7):4044-7. doi: 10.1073/pnas.77.7.4044.
Heats of thermal denaturation of chromatin core particles and core particles with covalently crosslinked histones were measured by differential scanning calorimetry. The additional stabilization of the nucleoprotein complex by crosslinking is not reflected in the transition enthalpy. The contribution of protein denaturation to the total heat was estimated by comparison of core particles with core particle DNA in a high-salt solution. By taking into account the temperature dependence of the transition enthalpy of DNA, we conclude that the enthalpy change for denaturation of DNA in core particles is nearly the same as that for naked DNA in solution.
通过差示扫描量热法测量了染色质核心颗粒以及组蛋白共价交联的核心颗粒的热变性热。交联对核蛋白复合物的额外稳定作用并未反映在转变焓中。通过比较高盐溶液中核心颗粒与核心颗粒DNA,估算了蛋白质变性对总热量的贡献。考虑到DNA转变焓的温度依赖性,我们得出结论,核心颗粒中DNA变性的焓变与溶液中裸露DNA的焓变几乎相同。