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首页> 外文期刊>Glycobiology. >Comparison of the methods for profiling glycoprotein glycans--HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study.
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Comparison of the methods for profiling glycoprotein glycans--HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study.

机译：糖蛋白聚糖谱图分析方法的比较-HUPO Human Disease Glycomics / Proteome Initiative多机构研究。

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Mass spectrometry (MS) of glycoproteins is an emerging field in proteomics, poised to meet the technical demand for elucidation of the structural complexity and functions of the oligosaccharide components of molecules. Considering the divergence of the mass spectrometric methods employed for oligosaccharide analysis in recent publications, it is necessary to establish technical standards and demonstrate capabilities. In the present study of the Human Proteome Organisation (HUPO) Human Disease Glycomics/Proteome Initiative (HGPI), the same samples of transferrin and immunoglobulin-G were analyzed for N-linked oligosaccharides and their relative abundances in 20 laboratories, and the chromatographic and mass spectrometric analysis results were evaluated. In general, matrix-assisted laser desorption/ionization (MALDI) time-of-flight MS of permethylated oligosaccharide mixtures carried out in six laboratories yielded good quantitation, and the results can be correlated to those of chromatography of reductive amination derivatives. For underivatized oligosaccharide alditols, graphitized carbon-liquid chromatography (LC)/electrospray ionization (ESI) MS detecting deprotonated molecules in the negative ion mode provided acceptable quantitation. The variance of the results among these three methods was small. Detailed analyses of tryptic glycopeptides employing either nano LC/ESI MS/MS or MALDI MS demonstrated excellent capability to determine site-specific or subclass-specific glycan profiles in these samples. Taking into account the variety of MS technologies and options for distinct protocols used in this study, the results of this multi-institutional study indicate that MS-based analysis appears as the efficient method for identification and quantitation of oligosaccharides in glycomic studies and endorse the power of MS for glycopeptide characterization with high sensitivity in proteomic programs.
机译：糖蛋白的质谱（MS）是蛋白质组学领域的一个新兴领域，有望满足阐明分子的寡糖组分的结构复杂性和功能的技术要求。考虑到最近出版物中用于寡糖分析的质谱方法的差异，有必要建立技术标准并证明其功能。在人类蛋白质组组织（HUPO）的人类疾病糖蛋白/蛋白质组计划（HGPI）的当前研究中，在20个实验室中分析了相同样本的转铁蛋白和免疫球蛋白G的N-连接寡糖及其相对丰度。评估了质谱分析结果。通常，在六个实验室中对全甲基化寡糖混合物进行基质辅助激光解吸/电离（MALDI）飞行时间质谱分析可获得良好的定量结果，其结果可与还原胺化衍生物色谱法相关。对于未衍生的低聚糖醛糖醇，石墨化碳液相色谱（LC）/电喷雾电离（ESI）MS以负离子模式检测去质子化的分子可提供可接受的定量。这三种方法之间的结果差异很小。使用纳米LC / ESI MS / MS或MALDI MS进行的胰蛋白酶糖肽的详细分析表明，在这些样品中确定位点特异性或亚类特异性聚糖谱的出色能力。考虑到本研究中使用的多种MS技术和不同方案的选项，该多机构研究的结果表明，基于MS的分析似乎是鉴定和定量糖化研究中寡糖的有效方法，并证明了其功效。 MS在蛋白质组学程序中以高灵敏度表征糖肽。

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