A strategy is presented for comparative analysis of glycoproteins in which the variation of protein concentration, variation of glycosylation site occupancy and variation of glycoform profile can be determined. A comparative study was performed using stable isotope labeling of glycopeptides and peptides by formaldehyde-H(2) and formaldehyde-D(2) and analysis by ESI-MS analysis. The relative intensity of the nonglycosylated peptide provided information about protein concentration variation. Variation of the glycoform profile was obtained by comparing the glycoform profile of d(0)- and d(4)-dimethyl labeled glycopeptides. By knowing the variation of protein concentration and the variation of glycoform profile, the variation of glycosylation site occupancy could be calculated. The utility of the proposed strategy was demonstrated with ribonuclease B with different protein concentrations, different levels of glycosylation site occupancy and different glycoform profiles.
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http://dx.doi.org/10.1016/j.aca.2012.03.058 | DOI Listing |
J Adv Res
December 2024
Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an 710069, China. Electronic address:
Introduction: The binding of the spike (S) protein of SARS-CoV-2 to angiotensin-converting enzyme 2 (ACE2) is a critical stage in the process of infection. While previous studies indicated that the S protein and ACE2 are extensively glycosylated, the functions of glycans in their interactions remain uncertain.
Objectives: This study aimed to investigate the glycan receptors of SARS-CoV-2 and evaluate the inhibitory effects of galactosylated glycoproteins derived from bovine milk on the attachment of SARS-CoV-2 pseudovirus.
J Immunol
December 2024
Division of Genetics, Department of Biology, Friedrich Alexander University Erlangen-Nuremberg, Erlangen, Germany.
The family of IgG Abs is a crucial component of adaptive immunity. Glycosylation of IgG maintains its structural integrity and modulates its effector functions. In this review, we discuss IgG glycosylation covering cell biological as well as therapeutic and disease-related aspects, focusing on the glycan structures in distinct IgG regions (Fab versus Fc).
View Article and Find Full Text PDFAnal Chim Acta
December 2024
University of Amsterdam, van 't Hoff Institute for Molecular Sciences, Analytical Chemistry Group, Science Park 904, 1098 XH, Amsterdam, the Netherlands; Centre of Analytical Sciences Amsterdam, Science Park 904, 1098 XH, Amsterdam, the Netherlands. Electronic address:
Biochim Biophys Acta Proteins Proteom
January 2025
Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Xinjiang Medical University, Urumqi 830017, China; Key Laboratory of Molecular Biology for Xinjiang Endemic Diseases, Urumqi 830017, China. Electronic address:
ACS Nano
October 2024
The Center for Clinical Molecular Medical Detection, The First Affiliated Hospital of Chongqing Medical University, Chongqing 400016, China.
Malignant transformation of cancer is often accompanied by aberrant glycopatterns. Epithelial-mesenchymal transition (EMT) is a crucial biological process in cancer migration and invasion, accelerating cancer deterioration. High-precision analysis of protein-glycan spatial profiling in the EMT process is essential for elucidating glycosylation functions and cancer progression.
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