Kolodzeĭskaia M V, Volkov G L
Palladin Institute of Biochemistry of National Academy of Sciences of Ukraine, Kyiv.
Ukr Biokhim Zh (1999). 2003 Sep-Oct;75(5):17-27.
Data concerning peculiarities of fermentative nature and structure of thrombin in water-salt solution have been generalized; regularities of stabilizing effect made on thrombin by various polyols and other substances have been analyzed. It has been shown that formation of thrombin optimum macrostructure is one of the methods of its stabilization. Presence of different dissolving additives changes this enzymes hydration and this affects its stability and activity. There exist some systems to stabilize thrombin solutions. The systems consist of various salts, low-molecular and high-molecular polyols, surfactants, protein chain, composition buffer, etc. It has been shown that optimal concentrations of polyols, buffer salts and surfactants, as well as protein interaction increase considerably thrombin stability, preserving secondary structure even under its low concentration in the solution.
关于凝血酶在水盐溶液中的发酵性质和结构特点的数据已得到汇总；分析了各种多元醇和其他物质对凝血酶的稳定作用规律。结果表明，形成凝血酶最佳宏观结构是其稳定化的方法之一。不同溶解添加剂的存在会改变这种酶的水合作用，进而影响其稳定性和活性。存在一些稳定凝血酶溶液的体系。这些体系由各种盐、低分子和高分子多元醇、表面活性剂、蛋白质链、组成缓冲液等组成。结果表明，多元醇、缓冲盐和表面活性剂的最佳浓度以及蛋白质相互作用可显著提高凝血酶的稳定性，即使在溶液中浓度较低时也能保持二级结构。
