离子交换高效液相色谱法研究巯基催化的牛巯基白蛋白结构变化
Ion-exchange high-performance liquid chromatographic studies on sulphydryl-catalysed structural alterations of bovine mercaptalbumin.
作者信息
Kuwata K, Era S, Inouye H, Sogami M, Sasaki H
出版信息
J Chromatogr. 1985 Sep 20;332:29-37. doi: 10.1016/s0021-9673(01)83284-2.
The N-A isomerization (the intramolecular SH/S-S exchange reaction) of bovine mercaptalbumin (BMA) in alkaline medium was studied by using ion-exchange high-performance liquid chromatography (HPLC) and moving-boundary electrophoresis. Results obtained by ion-exchange HPLC on the N-A isomerization of BMA were consistent with those by moving-boundary electrophoresis and showed at least two kinds of the A-form, A1 and A2, indicating that the N-A isomerization is a multi-step reaction. The rate of the N-A isomerization was strongly suppressed in [2H]water solution. The suppression by [2H]water might support the current view that intra- and intermolecular hydrophobic and/or hydrogen bonds are strengthened in [2H]water.
利用离子交换高效液相色谱法（HPLC）和移动界面电泳法，研究了碱性介质中牛巯基白蛋白（BMA）的N-A异构化反应（分子内SH/S-S交换反应）。离子交换HPLC法所得的关于BMA的N-A异构化反应结果与移动界面电泳法的结果一致，显示至少有两种A形式，即A1和A2，这表明N-A异构化是一个多步反应。在[2H]水溶液中，N-A异构化反应速率受到强烈抑制。[2H]水的抑制作用可能支持目前的观点，即在[2H]水中分子内和分子间的疏水和/或氢键会增强。
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