糖蛋白是重要的糖复合物，蛋白质糖基化修饰是蛋白质翻译后修饰的重要组成部分。与磷酸化、甲基化等修饰相比，蛋白质的糖基化位点不同和每个糖基化位点的糖链结构不同构成了糖基化修饰的"不均一性"。这种不均一性极大地限制了蛋白质糖基化修饰的分析，是糖组学领域中所面临的重大挑战。本课题组在已有的糖蛋白质组学和糖组学的研究基础上，结合凝集素快速识别、化学富集（氧化酰肼法SPEG）、和同位素标记的高分辨率质谱检测等技术，实现了快速灵敏的蛋白质糖基化修饰的定性定量分析，可以同时检测糖蛋白和糖多肽的氨基酸序列、糖基化位点、每个糖基化位点上的糖链特异性结构（motif）和分子表达水平。这种技术可以实现在人体血液组织等样品中的高通量分析，进而建立人体蛋白质特异性糖基化修饰数据库。作为新型的高通量糖组学分析技术，这种技术为基础研究和临床应用提供了有力的糖复合物分析工具和技术支持。

Glycosylation is the most common form of protein modifications. Each glycoprotein can be glycosylated at different glycosites and each glycosite may be modified by different glycans. This structural heterogeneity has complicated the study of the structure-function relationships of glycoproteins. In this study, we report a method for the rapid identification and quantification of the glycosylation on particular glycosites from complex biological mixtures using glycan-lectin affinity and chemical immobilization, followed by mass spectrometry. We showed the high-throughput identification of protein glycosylation in human plasma using this method. The application of this method may facilitate our understanding of how perturbed glycosylation impacts upon disease progression and could be used to discover glycosylated proteins that could serve as biomarkers or therapeutic targets to improve clinical outcomes of patients.