Protein refolding in predominantly organic media markedly enhanced by common salts.
Protein refolding in predominantly organic media markedly enhanced by common salts.
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食盐显着增强了蛋白质在有机介质中的重折叠。
DOI：
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发表时间：
1999
影响因子：
3.8
通讯作者：
A. Klibanov
中科院分区：
文献类型：
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作者：
R. V. Rariy;A. Klibanov
研究了未折叠/还原的蛋清溶菌酶在多种主要由溶解蛋白质的有机溶剂和水组成的非水介质中的再折叠/再氧化。人们发现，LiCl和其他普通盐在非水体系中显著（高达100倍以上）提高了溶菌酶的再折叠率，而在水中则降低了溶菌酶的再折叠率。这种令人惊讶的现象的机制似乎与盐诱导的非特异性溶菌酶聚集的抑制有关，因为盐增强了蛋白质的溶解度。
The refolding/reoxidation of unfolded/reduced hen egg-white lysozyme was investigated in a variety of predominantly nonaqueous media consisting of protein-dissolving organic solvents and water. It was discovered that LiCl and other common salts dramatically (up to more than 100-fold) increased the refolding yield of lysozyme in such nonaqueous systems, while reducing it in water. The mechanism of this surprising phenomenon appears to involve salt-induced suppression of nonspecific lysozyme aggregation during refolding due to an enhanced protein solubility.
追求蛋白质折叠。
DOI：
10.1126/science.8235606
发表时间：
1993
期刊：
Science (New York, N.Y.)
影响因子：
--
作者：
Englander,SW
通讯作者：
Englander,SW