OXIDATION OF SELENOMETHIONINE IN PEPTIDES BY HYDROGEN

氨基酸硒蛋氨酸已用于x射线检查。 结晶学作为一种标签来确定取代重的物相 金属衍生品。然而，在某些情况下， 含硒蛋氨酸蛋白质晶体的衍射性很差 模式。对这种现象的一种假设是，硒蛋氨酸 比蛋氨酸更容易被氧化。为了检验这一假设， 我们使用了基质辅助激光解吸质谱仪 测定过氧化氢产生的氧化产物 氧化。为了更好地表征对氧化的敏感性 多肽中的硒蛋氨酸残留量，我们用反相高效液相色谱法测定 定量分析氧化产物和在线高效液相色谱/电喷雾电离质谱仪 光谱分析来鉴定产品。通过这种方式，我们有了 表征了含硒蛋氨酸残基的氧化性能 多肽。一份描述这项工作的论文正在准备中。

The amino acid selenomethionine has been used in x-ray crystallography as a label to determine the phase in place of heavy metal derivatives. However, in some cases, the selenomethioninecontaining protein crystals give poor diffraction patterns. One hypothesis for this phenomenon is that selenomethionine is oxidized more easily than methionine. To examine this hypothesis, we have used matrix-assisted laser desorption mass spectrometry to determine the oxidized products generated by hydrogen peroxide oxidation. To better characterize the sensitivity to oxidation for selenomethionine residue in peptide, we employed reverse-phase HPLC to quantitatively analyze the oxidized products and on-line HPLC/ESI mass spectrometry to identify the products. By this means, we have characterized the oxidation properties of selenomethionine residue in peptide. A paper describing this work is in preparation.