Institute of Molecular Biology and Genetics, Seoul National University, Seoul, Republic of Korea.
J Chromatogr B Analyt Technol Biomed Life Sci. 2010 Dec 1;878(31):3323-6. doi: 10.1016/j.jchromb.2010.10.001. Epub 2010 Oct 12.
Lipopolysaccharide (LPS)-binding proteins interact with LPS in human serum and mediate various immune responses. We describe a high-throughput LPS-binding protein profiling platform for discovering unknown LPS-binding proteins and potential inflammatory mediators. As a pull-down method, the LPS molecules were immobilized onto epoxy beads and then directly incubated with human serum to screen LPS-binding proteins. Through the "untargeted" mass spectrometric approach, potential LPS-binding proteins which elicit various immune responses in human serum were identified by a highly sensitive LTQ Orbitrap Hybrid Fourier Transform Mass Spectrometer (LTQ Orbitrap FT MS). Therefore, this mass spectrometry (MS)-based profiling method is straightforward for screening unknown LPS-binding proteins and provides physiologically relevant binding partners in human serum.
脂多糖（LPS）结合蛋白与人血清中的 LPS 相互作用，介导各种免疫反应。我们描述了一种高通量的 LPS 结合蛋白分析平台，用于发现未知的 LPS 结合蛋白和潜在的炎症介质。作为一种下拉方法，将 LPS 分子固定在环氧珠上，然后直接与人血清孵育以筛选 LPS 结合蛋白。通过“非靶向”质谱方法，使用高灵敏度 LTQ Orbitrap 混合动力傅里叶变换质谱仪（LTQ Orbitrap FT MS）鉴定了在人血清中引发各种免疫反应的潜在 LPS 结合蛋白。因此，这种基于质谱（MS）的分析方法可直接用于筛选未知的 LPS 结合蛋白，并提供人血清中具有生理相关性的结合伴侣。
