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Related Concept Videos

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...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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...
Combinatorial Gene Control02:33

Combinatorial Gene Control

Combinatorial gene control is the synergistic action of several transcriptional factors to regulate the expression of a single gene. The absence of one or more of these factors may lead to a significant difference in the level of gene expression or repression.
The expression of more than 30,000 genes is controlled by approximately 2000-3000 transcription factors. This is possible because a single transcription factor can recognize more than one regulatory sequence. The specificity in gene...
Glycocalyx and its Functions01:14

Glycocalyx and its Functions

The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
Components of...
DNA Microarrays02:34

DNA Microarrays

Microarrays are high-throughput and relatively inexpensive assays that can be automated to analyze large quantities of data at a time. They are used in genome-wide studies to compare gene or protein expression under two varied conditions, such as healthy and diseased states. Microarrays consist of glass or silica slides on which probe molecules are covalently attached through surface functionalization. Most commonly, the slides are prepared through the chemisorption of silanes to silica...
Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...

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Related Experiment Video

Updated: May 27, 2026

Printed Glycan Array: A Sensitive Technique for the Analysis of the Repertoire of Circulating Anti-carbohydrate Antibodies in Small Animals
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Printed Glycan Array: A Sensitive Technique for the Analysis of the Repertoire of Circulating Anti-carbohydrate Antibodies in Small Animals

Published on: February 14, 2019

Combinatorial glycoarray.

Simon Rinaldi1, Kathryn M Brennan, Hugh J Willison

  • 1SRI International Biosciences Division, Menlo Park, CA, USA.

Methods in Molecular Biology (Clifton, N.J.)
|November 8, 2011
PubMed
Summary
This summary is machine-generated.

Researchers developed a semi-automated system to study how proteins bind to complex glycolipid mixtures. This new method allows for simultaneous analysis of numerous glycolipid complexes, advancing our understanding of crucial biological interactions.

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Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples
13:21

Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples

Published on: May 4, 2012

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Glycolipid-protein interactions are vital for immune recognition, cell signaling, and pathogen binding.
  • Current methods for studying these interactions often focus on single glycolipids, which may not reflect biological complexity.
  • Certain lectins and autoantibodies bind specifically to complexes of multiple gangliosides, necessitating new analytical approaches.

Purpose of the Study:

  • To develop a semi-automated system for high-throughput analysis of lectin binding to glycolipid complexes.
  • To overcome the technical challenges associated with investigating 1:1 glycolipid complexes.
  • To enable simultaneous assaying of lectin binding to numerous glycolipid complexes.

Main Methods:

  • Utilized an automated thin-layer chromatography sampler to prepare glycolipid complexes in microvials.
  • Printed reproducible arrays of glycolipid complexes (up to 300 spots/slide) onto polyvinylidene difluoride membranes on glass slides.
  • Probed arrays with lectins, followed by detection using a horseradish peroxidase-linked secondary antibody and chemiluminescence.

Main Results:

  • Successfully developed a semi-automated system for printing dense arrays of glycolipid complexes.
  • Demonstrated the capability to assay lectin binding to numerous glycolipid complexes simultaneously.
  • Established a method for quantifying lectin binding through image analysis of signal intensity.

Conclusions:

  • The developed system offers a robust and efficient method for studying complex glycolipid-protein interactions.
  • This technology facilitates the investigation of lectin binding to heterodimeric glycolipid complexes.
  • The semi-automated approach enhances the study of biologically relevant glycolipid interactions.