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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,...
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...
Overview Of Cell Separation And Isolation01:20

Overview Of Cell Separation And Isolation

Cell separation was first achieved in 1964 by S. H. Seal, who separated large tumor cells from the smaller blood cells using filtration. Two years later, Pohl and Hawk performed experiments on how cells respond differently to a nonuniform electric field based on the cell type. Such observations were the inception of cell separation methods, which allow isolating a single cell type from a heterogeneous sample.
Glycosaminoglycans01:23

Glycosaminoglycans

Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
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...
Types Of Column Chromatography01:29

Types Of Column Chromatography

The stability and compatibility of column material with samples are crucial for efficient purification in chromatographic techniques. Various operating parameters such as pH, temperature, or solvent affect the packing of the column material, thereby determining the purification efficiency. The choice of column material also plays an essential role in deciding the operating parameters and can be modified based on the proteins that need to be purified.
Gel Filtration Chromatography
When the...

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Related Experiment Video

Updated: Jul 5, 2026

Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry
14:02

Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry

Published on: April 21, 2017

Extraction and separation of proteoglycans.

Masaki Yanagishita1, Katarzyna Anna Podyma-Inoue, Miki Yokoyama

  • 1Biochemistry, Department of Hard Tissue Engineering, Graduate School, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8549, Japan. m.yanagishita.bch@tmd.ac.jp

Glycoconjugate Journal
|May 22, 2008
PubMed
Summary

Proteoglycans, featuring unique glycosaminoglycans, bind diverse molecules via specific sulfate arrangements. Anion exchange chromatography is a key method for separating these complex molecules from tissues.

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Detection of Glycosaminoglycans by Polyacrylamide Gel Electrophoresis and Silver Staining

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Last Updated: Jul 5, 2026

Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry
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Published on: April 21, 2017

A Quantitative Glycomics and Proteomics Combined Purification Strategy
11:38

A Quantitative Glycomics and Proteomics Combined Purification Strategy

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Detection of Glycosaminoglycans by Polyacrylamide Gel Electrophoresis and Silver Staining
05:57

Detection of Glycosaminoglycans by Polyacrylamide Gel Electrophoresis and Silver Staining

Published on: February 25, 2021

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Proteoglycans possess unique glycosaminoglycan (GAG) components with repeating, sulfated disaccharides.
  • Specific sulfate clustering on GAGs creates binding sites for extracellular matrix molecules and growth factors.
  • Proteoglycan core proteins mediate interactions for extracellular matrix organization and cell membrane anchoring.

Purpose of the Study:

  • To highlight the molecular interactions of proteoglycans.
  • To discuss methods for proteoglycan extraction and separation.

Main Methods:

  • Extraction protocols involve denaturing solvents to disrupt molecular interactions.
  • Anion exchange chromatography is presented as a primary separation technique.

Main Results:

  • Proteoglycans interact with various molecules through their GAGs and core proteins.
  • Denaturing solvents are necessary for efficient proteoglycan extraction.
  • Anion exchange chromatography effectively separates proteoglycans based on their negatively charged GAGs.

Conclusions:

  • Proteoglycans play crucial roles in molecular interactions and tissue organization.
  • Effective extraction and separation methods are essential for studying proteoglycans.
  • Anion exchange chromatography offers a convenient and general approach for proteoglycan separation.