PREFERENTIAL INTERACTIONS OF PROTEINS WITH SALTS IN CONCENTRATED-SOLUTIONS
PREFERENTIAL INTERACTIONS OF PROTEINS WITH SALTS IN CONCENTRATED-SOLUTIONS
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DOI：
10.1021/bi00268a034
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发表时间：
1982-01-01
期刊：
影响因子：
2.9
通讯作者：
TIMASHEFF, SN
中科院分区：
文献类型：
--
作者：
ARAKAWA, T;TIMASHEFF, SN
用密度法研究了浓盐中蛋白质与溶剂组分的优先相互作用。蛋白质在NaCl、NaCH3COO和Na2SO4中优先水化。由此产生的不利的自由能变化与这些盐对蛋白质的溶解度和稳定性的影响有关。这种不利的自由能变化与这些盐的大的、正的表面张力增量有关，即它们对表面自由能的扰动。另一方面，KSCN、CaCl2和MgCl2与牛血清白蛋白表现出相当大的结合，这可能与它们对大分子的不稳定和盐化作用有关。由于后两种盐具有较高的表面张力增量，这并不一定导致蛋白质优先水化和稳定。
The preferential interactions of proteins with solvent components were studied in concentrated salt by densimetric measurements. Proteins were preferentially hydrated in NaCl, NaCH3COO, and Na2SO4. The resulting unfavorable free-energy change was related to the effects of these salts on solubility and stability of the proteins. This unfavorable free-energy change was correlated with the large, positive surface tension increment of these salts, i.e., their perturbation of surface free energy. On the other hand, KSCN, CaCl2 and MgCl2 showed considerable binding to bovine serum albumin, which could be related to their destabilizing and salting-in effects on macromolecules. Since the last 2 salts have high surface tension increments, this does not necessarily lead to protein preferential hydration and stabilization.