Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Free Radic Biol Med. 2012 Sep 15;53(6):1222-5. doi: 10.1016/j.freeradbiomed.2012.06.036. Epub 2012 Jul 3.
Methionine residues in protein can be oxidized by reactive oxygen or nitrogen species to generate methionine sulfoxide. This covalent modification has been implicated in processes ranging from normal cell signaling to neurodegenerative diseases. A general method for detecting methionine sulfoxide in proteins would be of great value in studying these processes, but development of a chemical or immunochemical technique has been elusive. Recently, an antiserum raised against an oxidized corn protein, DZS18, was reported to be specific for methionine sulfoxide in proteins (Arch. Biochem. Biophys. 485:35-40; 2009). However, data included in that report indicate that the antiserum is not specific. Utilizing well-characterized native and methionine-oxidized glutamine synthetase and aprotinin, we confirm that the antiserum does not possess specificity for methionine sulfoxide.
蛋白质中的蛋氨酸残基可被活性氧或氮物种氧化生成蛋氨酸亚砜。这种共价修饰与从正常细胞信号传递到神经退行性疾病的各种过程有关。一种用于检测蛋白质中蛋氨酸亚砜的通用方法对于研究这些过程将具有重要价值,但化学或免疫化学技术的开发一直难以实现。最近,据报道,针对氧化玉米蛋白 DZS18 产生的抗血清特异性针对蛋白质中的蛋氨酸亚砜(Arch. Biochem. Biophys. 485:35-40; 2009)。然而,该报告中的数据表明该抗血清不具有特异性。利用经过充分表征的天然和蛋氨酸氧化谷氨酰胺合成酶和抑肽酶,我们证实该抗血清不具有蛋氨酸亚砜特异性。