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

Proteoglycans01:05

Proteoglycans

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,...
Protein Glycosylation01:25

Protein Glycosylation

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...

You might also read

Related Articles

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

Sort by
Same author

A new and eco-friendly disinfectant for antimicrobial-resistant bacteria: ozone nano water.

BMC microbiology·2026
Same author

Sustainable Bamboo-Based Magnetic Activated Carbon for Adsorption of Cationic and Anionic Dyes from Wastewater: Kinetics, Isotherms, and Thermodynamics.

Materials (Basel, Switzerland)·2026
Same author

Assessment of Acetabular Fracture Fixation with the Modified Harris Hip Score Regarding Clinical and Functional Outcomes.

Journal of the College of Physicians and Surgeons--Pakistan : JCPSP·2026
Same author

Physiological architecture and evolutionary origins of cellular adaptability.

bioRxiv : the preprint server for biology·2026
Same author

Potential Involvement of Fructosylated Human Insulin and Serological Evidence in Subclinical Autoimmune Activity in Type 2 Diabetes Mellitus.

Current diabetes reviews·2026
Same author

Postparathyroidectomy calciphylaxis in a patient with primary hyperparathyroidism: a rare complication.

JCEM case reports·2026

Related Experiment Video

Updated: May 25, 2026

Immunoglobulin G N-Glycan Analysis by Ultra-Performance Liquid Chromatography
11:01

Immunoglobulin G N-Glycan Analysis by Ultra-Performance Liquid Chromatography

Published on: January 18, 2020

Physicochemical studies on glycation-induced structural changes in human IgG.

Saman Ahmad1, Moinuddin, Rizwan Hasan Khan

  • 1Department of Biochemistry, Faculty of Medicine, J.N. Medical College, Aligarh Muslim University, Aligarh, UP, India.

IUBMB Life
|January 14, 2012
PubMed
Summary
This summary is machine-generated.

Glycation modifies immunoglobulin G (IgG), forming advanced glycation end products (AGEs). This structural change in IgG may contribute to rheumatoid arthritis (RA) and could serve as an early diagnostic biomarker.

More Related Videos

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Analyzing the Permeability of the Blood-Brain Barrier by Microbial Traversal through Microvascular Endothelial Cells
06:26

Analyzing the Permeability of the Blood-Brain Barrier by Microbial Traversal through Microvascular Endothelial Cells

Published on: February 14, 2020

Related Experiment Videos

Last Updated: May 25, 2026

Immunoglobulin G N-Glycan Analysis by Ultra-Performance Liquid Chromatography
11:01

Immunoglobulin G N-Glycan Analysis by Ultra-Performance Liquid Chromatography

Published on: January 18, 2020

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Analyzing the Permeability of the Blood-Brain Barrier by Microbial Traversal through Microvascular Endothelial Cells
06:26

Analyzing the Permeability of the Blood-Brain Barrier by Microbial Traversal through Microvascular Endothelial Cells

Published on: February 14, 2020

Area of Science:

  • Biochemistry
  • Immunology
  • Molecular Biology

Background:

  • Glycation of biomolecules produces advanced glycation end products (AGEs).
  • Glycation of immunoglobulin G (IgG) is linked to autoimmune diseases like rheumatoid arthritis (RA).

Purpose of the Study:

  • To investigate structural and functional changes in human IgG upon glycation with glucose.
  • To explore the potential of glycated IgG as a biomarker for rheumatoid arthritis.

Main Methods:

  • Human IgG was glycated using physiological glucose concentrations.
  • Analysis involved UV, fluorescence, circular dichroism, FTIR spectroscopy, thermal denaturation, and gel electrophoresis.
  • Quantification of ketoamine moieties and carbonyl content in glycated IgG.

Main Results:

  • Glycation induced structural perturbations in IgG.
  • Increased carbonyl content and ketoamine moieties were observed in glycated IgG.
  • These modifications suggest potential interference with normal IgG function.

Conclusions:

  • Glycated IgG exhibits altered structure and composition.
  • These changes may contribute to the pathogenesis of arthritic conditions.
  • AGEs-modified IgG shows promise as a biomarker for early RA detection.