Department of Chemistry and Biochemistry, Faculty of Agronomy, Mendel University of Agriculture and Forestry, CZ-613 00 Brno, Czech Republic.
Electrophoresis. 2009 Dec;30(23):4029-33. doi: 10.1002/elps.200900226.
Metallothionein (MT) is a low-molecular mass protein playing an essential role in homeostasis of heavy metals ions. We used a chip-based CE for quantitative study of MT oxidation. After oxidation of MT by H(2)O(2) we observed marked decrease in peaks heights and shift of peaks positions to higher molecular mass, which corresponded with the time of the oxidation. Moreover, we observed that the proportion of high-molecular forms of MT was markedly increased. The oxidative changes were successfully reversed by using of reducing agent prior to electrophoresis. Our method can reveal the stability MT aggregates, of which biological role still remains unclear.
金属硫蛋白（MT）是一种低分子量的蛋白质，在重金属离子的体内平衡中起着至关重要的作用。我们使用基于芯片的 CE 技术对 MT 的氧化进行定量研究。在 MT 被 H(2)O(2)氧化后，我们观察到峰高明显降低，并且峰位置向更高的分子量移动，这与氧化时间相对应。此外，我们还观察到 MT 的高分子形式的比例明显增加。在电泳前使用还原剂可以成功逆转氧化变化。我们的方法可以揭示 MT 聚集体的稳定性，其生物学作用尚不清楚。
