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Analytical progress for protein glycosylation in China

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Frontiers of Chemistry in China

Abstract

Glycosylation plays a key role in controlling various cellular processes; in diseases modifications of the glycans also highlight its clinical importance. However, ^glycosylation analysis remains a difficult task. In recent years, ^advances in sample preparation and mass spectrometry have greatly facilitated the analysis of glycoproteins. This review mainly covers five aspects of the improvements and advances on the research of protein glycosylation in China: 1) identification of glycoproteins, ^2) identification of glycosylation sites, ^3) new methods developed for glycopeptides enrichment, ^4) characterization of glycans, ^and 5) functional studies of protein glycosylation.

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Authors and Affiliations

  1. Institutes of Biomedical Sciences & Department of Chemistry, Fudan University, Shanghai, 200032, China

    Jing Cao, Yaohan Chen & Pengyuan Yang

Authors
  1. Jing Cao
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  2. Yaohan Chen
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  3. Pengyuan Yang
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Corresponding author

Correspondence to Pengyuan Yang.

Additional information

Pengyuan YANG got his B. S. degree from the Inner Mongoliar University and his Master’s degree from University of Science and Technology of China. He studied for his Ph.D. degree at the University of Massachussetts with Dr. R. M. Barnes. After got his Ph. D. degree in 1987, he did several post-doc researches, including at Indiana University (with Dr. G. M. Hieftje) and Xiamen University (with Prof. B. L. Huang). He is now a professor and Ph.D. supervisor in the Institutes of Biomedical Sciences and Deptartment of Chemistry, Fudan University. Prof. Yang’s research interests include disease proteomics, protein post modification (e.g. glycosylation), biomass spectrometer and biomass spectrometry hyphenated technology and interface theory and technology, artificial alfactory and new pricinple for biomolecule determination.

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Cao, J., Chen, Y. & Yang, P. Analytical progress for protein glycosylation in China. Front. Chem. China 4, 360–367 (2009). https://doi.org/10.1007/s11458-009-0107-7

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  • DOI: https://doi.org/10.1007/s11458-009-0107-7

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