首页> 外文会议>American Society for Mass Spectrometry Conference on Mass Spectrometry and Allied Topics >Glycosylation Profiling of Therapeutically Active Glycoproteins: Identification of Glycans in Recombinant Factor IX using Directed MALDI-QIT-TOF-MS~(n) and a Glycan Database
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Glycosylation Profiling of Therapeutically Active Glycoproteins: Identification of Glycans in Recombinant Factor IX using Directed MALDI-QIT-TOF-MS~(n) and a Glycan Database

机译:治疗活性糖蛋白的糖基化分析:使用指向MALDI-QIT-TOF-MS〜(n)和甘草数据库的重组因子IX中聚糖的鉴定

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We have tested our Accurate Glycan Analyser workflow by easily detecting and identifying glycans from known glycoproteins, such as fetuin. We have shown one application aimed at the quality control of therapeutically active glycoproteins (blood coagulation Factor IX). It is a challenge nowadays to produce recombinant, therapeutically active glycoproteins. Our example demonstrate this fact, as significant differences were observed between plasma-derived- and recombinant-FIX: the extent of fucosylation and the core structures of the identified glycans were the main inconsistencies between these two endogenous glycoproteins.
机译:我们通过易于检测和识别来自已知糖蛋白的聚糖,例如蕨类植物来测试我们的精确聚糖分析仪工作流程。我们已经显示了一个旨在治疗活性糖蛋白(血液凝固因子IX)的质量控制的应用。现在是产生重组,治疗活性糖蛋白的挑战。我们的例子证明了这一事实,因为在血浆衍生和重组固定之间观察到显着差异:岩藻糖基化的程度和所鉴定的聚糖的核心结构是这两个内源性糖蛋白之间的主要不一致。

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