Thermodynamic stability of proteins in salt solutions: A comparison of the effectiveness of protein stabilizers
Thermodynamic stability of proteins in salt solutions: A comparison of the effectiveness of protein stabilizers
复制标题
盐溶液中蛋白质的热力学稳定性：蛋白质稳定剂有效性的比较
DOI：
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发表时间：
1986
期刊：
影响因子：
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通讯作者：
C. Bigelow
中科院分区：
文献类型：
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作者：
F. Ahmad;C. Bigelow
研究了不同浓度的稳定盐，即磷酸钾、硫酸铵和醋酸钾对盐酸胍对蛋白质的变性作用。在pH值为7.0和25°C时，观察了多肽圆二色谱的变化，从而确定了天然⇄变性过程中的稳定自由能。结果表明，阴离子的稳定能力按醋酸盐<；硫酸盐<；磷酸盐的顺序增加，与阴离子溶致系列一致。核糖核酸酶A已知有一个可以结合磷酸或硫酸盐离子的位点，它对这些阴离子的稳定作用比对溶菌酶、胃蛋白酶原和肌红蛋白的稳定作用更大。
The denaturation of proteins by guanidine hydrochloride was studied in the presence of different concentrations of stabilizing salts, namely potassium phosphate, ammonium sulfate, and potassium acetate. The denaturation transition was followed by observing changes in the peptide circular dichroism atpH 7.0 and 25°C. From these results the free energy of stabilization for the process native ⇄ denatured was determined. It was found that the stabilizing power of the anions increased in the order acetate < sulfate < phosphate, in agreement with the anionic lyotropic series. Ribonuclease A, which is known to have a site that can bind either a phosphate or a sulfate ion, showed a larger stabilization by these anions than that for lysozyme, pepsinogen, and myoglobin.
计算浓盐和氨基酸溶液中蛋白质的部分比容。
影响因子：
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作者：
Arakawa,T;Timasheff,SN
通讯作者：
Timasheff,SN