Related Experiment Video

Updated: Aug 9, 2026

Using Unfixed, Frozen Tissues to Study Natural Mucin Distribution
11:39

Using Unfixed, Frozen Tissues to Study Natural Mucin Distribution

Published on: September 21, 2012

Characterization of glycoconjugates in the human cameral mucous gel by lectins

F J Carreras1, D Porcel, J J López-Caballero

  • 1Department of Surgery (Ophthalmology), Faculty of Medicine, University of Granada, Spain.

Ophthalmic Research
|January 1, 1994
PubMed

A cameral mucous gel (CMG) has been described in human eyes lining the anterior and posterior ocular chambers. We assay a battery of 11 lectins to characterize the accessible sugars of the presumed glycoproteins and glycosaminoglycans present in the gel. Results show a predominance of alpha-linked sugars over beta-linked ones. There is evidence for the prominence in the gel of alpha-N-acetyl-D-galactosamine and/or alpha-D-galactose, together with alpha-N-acetyl-glucosamine. The second most important sugars are beta-N-acetyl-D-glucosamine and the dissacharide beta-D-galactose-N-acetyl-D-galactosamine. beta-N-acetyl-galactosamine could possibly be identified in third place. Neither fucose nor mannose are detected. These results point towards heparan and perlecan as possible components of the glycidic fraction of the gel, although a specific proteoglycan adapted to the osmotic role of the CMG is not at all unlikely.

More Related Videos

Rapid Glyco-Qualitative Assessment of Recombinant Proteins Using a Fully Automated System05:19

Rapid Glyco-Qualitative Assessment of Recombinant Proteins Using a Fully Automated System

Published on: June 28, 2024

Profiling of Permethylated Mucin O-glycans Using Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry08:51

Profiling of Permethylated Mucin O-glycans Using Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry

Published on: June 20, 2025

Related Concept Videos

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...
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,...
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...
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...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
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...