Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

6.9K
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
6.9K
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

2.9K
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
2.9K
Proteoglycans01:05

Proteoglycans

3.9K
Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
3.9K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Metagenomic insights into microbial drivers of organic micropollutant removal in wastewater-impacted riverbank filtration.

Water research·2026
Same author

Tumor sialylation regulates G-CSF stability and promotes neutrophil-mediated immunosuppression in breast cancer.

Nature communications·2026
Same author

Glycine-mediated microbial interactions in biological phosphorus removal systems.

Water research·2026
Same author

Erratum to "Extracellular polymeric substances in aerobic granular sludge under increasing salinity conditions" [Water Research (2026) 292/125313].

Water research·2026
Same author

Sequential Oxidizing-Reducing Degradation of Organic Micropollutants in Simulated Riverbank Filtration.

Environmental science & technology·2026
Same author

Molecular basis for anti-jumbo phage immunity by AVAST type 5.

Molecular cell·2026

Related Experiment Video

Updated: Jul 6, 2025

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling
11:08

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling

Published on: February 5, 2018

8.7K

Simple Routes to Stable Isotope-Coded Native Glycans.

Johannes Helm1, Clemens Grünwald-Gruber1, Jonathan Urteil1

  • 1Department of Chemistry, University of Natural Resources and Life Sciences Vienna, Muthgasse 18, 1190 Vienna, Austria.

Analytical Chemistry
|December 28, 2023
PubMed
Summary

A new method uses hydrazine hydrate for stable isotope labeling of glycans, enabling better identification and isomer separation for biological studies. This approach offers a safer and more affordable way to create essential glycan standards.

More Related Videos

Regioselective O-Glycosylation of Nucleosides via the Temporary 2',3'-Diol Protection by a Boronic Ester for the Synthesis of Disaccharide Nucleosides
08:46

Regioselective O-Glycosylation of Nucleosides via the Temporary 2',3'-Diol Protection by a Boronic Ester for the Synthesis of Disaccharide Nucleosides

Published on: July 26, 2018

8.7K
Hierarchical and Programmable One-Pot Oligosaccharide Synthesis
09:56

Hierarchical and Programmable One-Pot Oligosaccharide Synthesis

Published on: September 6, 2019

6.8K

Related Experiment Videos

Last Updated: Jul 6, 2025

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling
11:08

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling

Published on: February 5, 2018

8.7K
Regioselective O-Glycosylation of Nucleosides via the Temporary 2',3'-Diol Protection by a Boronic Ester for the Synthesis of Disaccharide Nucleosides
08:46

Regioselective O-Glycosylation of Nucleosides via the Temporary 2',3'-Diol Protection by a Boronic Ester for the Synthesis of Disaccharide Nucleosides

Published on: July 26, 2018

8.7K
Hierarchical and Programmable One-Pot Oligosaccharide Synthesis
09:56

Hierarchical and Programmable One-Pot Oligosaccharide Synthesis

Published on: September 6, 2019

6.8K

Area of Science:

  • Glycomics
  • Mass Spectrometry
  • Carbohydrate Chemistry

Background:

  • Accurate identification of glycans is crucial for understanding their biological roles.
  • Stable isotope-labeled glycans are vital for retention time normalization in mass spectrometry-based glycan analysis.
  • Current methods for producing labeled glycans involve chemoenzymatic or enzymatic approaches, which can be complex or introduce specific labels.

Purpose of the Study:

  • To develop a more accessible and safer method for introducing stable isotopes into glycans.
  • To enable the creation of mass-encoded glycans for advanced analytical applications.
  • To provide a versatile platform for generating glycan standards for isomer-specific studies.

Main Methods:

  • De-N-acetylation of glycans using hydrazine hydrate, a less hazardous and more affordable reagent than anhydrous hydrazine.
  • Optimization of reaction conditions (time, temperature) for complete conversion and isolation of intermediate products.
  • Introduction of heavy isotopes into the de-N-acetylated glycans to create mass-encoded standards.

Main Results:

  • Hydrazine hydrate effectively achieves de-N-acetylation, enabling heavy isotope incorporation.
  • Complete conversion of biantennary glycans (with or without sialic acids) is achieved in 72 hours at 100 °C.
  • Shorter incubation times allow for the isolation of intermediates with defined degrees of free amino groups, enabling variable isotope incorporation.

Conclusions:

  • The described method provides a versatile and cost-effective route to mass-encoded glycans.
  • These labeled glycans can serve as internal standards for isomer-specific LC-MS analysis of various glycan types, including N-glycans, O-glycans, and human milk oligosaccharides.
  • This approach enhances the reliability and scope of glycan analysis in biological research.