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Glycoproteins obtained from cell culture supernatants or lysates generally exist as mixtures of over 100 differently glycosylated protein forms (glycoforms). The study of glycosylation is significantly impeded because of the heterogeneous nature of glycoproteins. To overcome this challenge, we developed and optimized a glycoform library-based strategy to investigate the role of protein glycosylation. In this strategy, chemical synthesis was used to prepare individual homogeneous glycoforms and the role of glycosylation was determined by comparing a series of glycoforms with systematic differences in their glycosylation patterns.
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http://dx.doi.org/10.1007/978-1-0716-2489-0_14 | DOI Listing |
Methods Mol Biol
June 2022
State Key Laboratory of Bioactive Substance and Function of Natural Medicines, Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China.
Glycoproteins obtained from cell culture supernatants or lysates generally exist as mixtures of over 100 differently glycosylated protein forms (glycoforms). The study of glycosylation is significantly impeded because of the heterogeneous nature of glycoproteins. To overcome this challenge, we developed and optimized a glycoform library-based strategy to investigate the role of protein glycosylation.
View Article and Find Full Text PDFAnal Chem
January 2020
National Center for Protein Sciences Beijing, State Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Lifeomics, Beijing 102206 , People's Republic of China.
Protein -glycosylation has long been recognized to be closely associated with many diseases, particularly with tumor proliferation, invasion, and metastasis. The ability to efficiently profile the variation of -glycosylation in large-scale clinical samples provides an important approach for the development of biomarkers for cancer diagnosis and for therapeutic response evaluation. Therefore, mass spectrometry (MS)-based techniques for high throughput, in-depth and reliable elucidation of protein -glycosylation in large clinical cohorts are in high demand.
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