L-Arginine increases the solubility of unfolded species of hen egg white lysozyme
L-Arginine increases the solubility of unfolded species of hen egg white lysozyme
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DOI：
10.1110/ps.041085005
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发表时间：
2005-04-01
期刊：
影响因子：
8
通讯作者：
Lange, C
中科院分区：
文献类型：
--
作者：
Reddy, RC;Lilie, H;Lange, C
L-精氨酸(L-精氨酸)被广泛用作蛋白质复性的促进剂。其行动背后的机制仍不完全清楚。以鸡蛋清溶菌酶为模型蛋白，我们提供的数据清楚地证明了L-精氨酸对变性蛋白聚集的抑制作用。通过对游离半胱氨酸的化学修饰，获得了一系列未折叠的溶菌酶物种，作为氧化复性过程中未折叠和中间态的模型。在L-精氨酸存在下，展开物种和中间体的平衡溶解度增加似乎是其主要作用机制。
L-Arginine (L-Arg) has been widely used as an enhancer of protein renaturation. The mechanism behind its action is still not fully understood. Using hen egg white lysozyme as a model protein, we present data that clearly demonstrate the suppression of the aggregation of denatured protein by L-Arg. By chemical modification of free cysteines, a series of unfolded lysozyme species were obtained that served as models for unfolded and intermediate states during the process of oxidative refolding. An increased equilibrium solubility of unfolded species and intermediates in the presence of L-Arg seems to be its major mechanism of action.