Grigorian K R, Shiladzhian A A
Armenian State University, Yerevan, Armenia.
Bioorg Khim. 2009 Sep-Oct;35(5):646-9. doi: 10.1134/s1068162009050070.
The effects of solvated ions on the thermal denaturation of human serum albumin (HAS) in water-dimethylsulfoxide (DMSO) solutions were studied by the method of electron absorption spectroscopy. It was shown that depending on the DMSO concentration, electrolytes (LiCl, LiNO3, LiClO4, NaCl, and NaNO3) contained in these solutions were characterized by different anion and cation solvation degrees: unlike cations, anions were only negligibly solvated, which affected HAS thermal denaturation. Electrostatic interactions between anions and positively charged amino acid residues supporting protein denaturation subsided in the line Cl- > NO3- > ClO4-.
采用电子吸收光谱法研究了溶剂化离子对人血清白蛋白（HAS）在水 - 二甲基亚砜（DMSO）溶液中热变性的影响。结果表明，根据DMSO浓度，这些溶液中所含电解质（LiCl、LiNO3、LiClO4、NaCl和NaNO3）具有不同的阴离子和阳离子溶剂化程度：与阳离子不同，阴离子的溶剂化程度可忽略不计，这影响了HAS的热变性。支持蛋白质变性的阴离子与带正电荷氨基酸残基之间的静电相互作用在Cl- > NO3- > ClO4-序列中减弱。
