Institute of Bioorganic Chemistry, Polish Academy of Sciences, 61-704 Poznań, Poland.
Anal Biochem. 2010 Oct 1;405(1):132-4. doi: 10.1016/j.ab.2010.04.034. Epub 2010 Jul 5.
A posttranslational protein modification by homocysteine-thiolactone (N-homocysteinylation) is linked to human vascular and neurodegenerative diseases. Although chemical and immunological methods are available to detect and quantify the extent of protein N-homocysteinylation, the determination of site-specific N-homocysteinylation in vivo remains challenging. Here we describe a liquid chromatography/mass spectrometry method that monitors the extent of N-homocysteinylation at albumin lysine-525 in vivo directly in human serum. Using this method, we found that the extent of lysine-525 N-homocysteinylation was significantly increased in patients with cystathionine beta-synthase deficiency.
同型半胱氨酸-硫内酯（N-同型半胱氨酸化）对蛋白质的翻译后修饰与人类血管和神经退行性疾病有关。尽管有化学和免疫学方法可用于检测和定量蛋白质的 N-同型半胱氨酸化程度，但体内特定位置的 N-同型半胱氨酸化的测定仍然具有挑战性。在这里，我们描述了一种液相色谱/质谱法，可直接在人血清中监测体内白蛋白赖氨酸-525 的 N-同型半胱氨酸化程度。使用该方法，我们发现胱硫醚-β-合酶缺乏症患者的赖氨酸-525 N-同型半胱氨酸化程度显著增加。
