scholarly journals Sialic acid derivatization for glycan analysis by mass spectrometry

2019 ◽  
Vol 95 (9) ◽  
pp. 523-537 ◽  
Author(s):  
Takashi NISHIKAZE
2021 ◽  
Author(s):  
Yixuan Xie ◽  
Siyu Chen ◽  
Qiongyu Li ◽  
Ying Sheng ◽  
Michael R Alvarez ◽  
...  

A cross-linking method is developed to elucidate the glycan-mediated interactions between membrane proteins through sialic acids. The method provides previously unknown extensive glycomic interactions on cell membranes. The vast majority...


2021 ◽  
Author(s):  
Katerina Djambazova ◽  
Martin Dufresne ◽  
Lukasz Migas ◽  
Angela Kruse ◽  
Raf Van de Plas ◽  
...  

Gangliosides are classified as acidic glycosphingolipids, containing ceramide moieties and oligosaccharide chains with one or multiple sialic acid residue(s). The presence of multiple sialylation sites gives rise to highly diverse isomeric structures with distinct biological roles. Matrix-assisted laser desorption/ionization imaging mass spectrometry (MALDI IMS) enables the untargeted spatial analysis of gangliosides, among other biomolecules, directly from tissue sections. Integrating trapped ion mobility mass spectrometry (TIMS), a gas-phase separation technology, with MALDI IMS allows for the investi-gation of isomeric lipid structures in situ. Here we demonstrate the gas-phase separation of disialoganglioside isomers GD1a and GD1b that differ in the position of a sialic acid residue, in a standard mixture of both isomers, a total ganglioside extract, and directly from thin tissue sections. The unique spatial distributions of GD1a/b (d36:1) and GD1a/b (d38:1) were deter-mined from rat hippocampus, as well as in a spinal cord tissue section.


The Analyst ◽  
2020 ◽  
Vol 145 (5) ◽  
pp. 1737-1748
Author(s):  
Alessandro Quaranta ◽  
Maya Spasova ◽  
Elena Passarini ◽  
Isabella Karlsson ◽  
Lorena Ndreu ◽  
...  

Glycosylation characterization could lead to the discovery of biomarkers and is crucial in quality control of biopharmaceuticals. Here we present a method to quantify glycoforms on intact proteins, with parallel glycan identification by IMS-MS/MS.


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