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Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system

机译:使用免疫球蛋白G作为模型系统的糖蛋白稳定同位素辅助NMR方法

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A paper published in Progress in Nuclear Magnetic Resonance Spectroscopy informs about stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G (IgG) as a model system. The paper describes about the application of the stable-isotope-assisted NMR approach to structural analyses of glycoprotein glycans using IgG as a model system. IgG is described as a multi-domain glycoprotein with a molecular mass of 150 kDa, functioning as the major class of antibodies in the immune system. Three-dimensional structures have been determined by X-ray crystallographic analyses and are available for intact IgG molecules and for a proteolytic fragment Fc. Two methods are employed for stable-isotope-labeling of IgG-Fc glycans. These two methods include metabolic labeling through biosynthetic pathways of production vehicles and in vitro enzymatic attachment of isotopically labeled monosaccharide(s) onto the non-reducing end of the Fc glycans.
机译:发表在《核磁共振光谱学进展》上的一篇论文介绍了使用免疫球蛋白G(IgG)作为模型系统的糖蛋白的稳定同位素辅助NMR方法。本文介绍了使用IgG作为模型系统的稳定同位素辅助NMR方法在糖蛋白聚糖结构分析中的应用。 IgG被描述为分子量为150 kDa的多结构域糖蛋白,在免疫系统中起主要抗体类别的作用。三维结构已通过X射线晶体学分析确定,可用于完整的IgG分子和蛋白水解片段Fc。采用两种方法对IgG-Fc聚糖进行稳定同位素标记。这两种方法包括通过生产载体的生物合成途径进行代谢标记,以及将同位素标记的单糖体外酶附在Fc聚糖的非还原端上。

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