Related Experiment Video

Updated: Aug 12, 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

A soybean lectin having 4-O-methyl-D-glucuronic acid specificity

M A Dombrink-Kurtzman, W E Dick, K A Burton

    Biochemical and Biophysical Research Communications
    |March 29, 1983
    PubMed

    More Related Videos

    Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions11:21

    Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

    Published on: January 20, 2022

    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

    Related Concept Videos

    Ligand Binding Sites02:40

    Ligand Binding Sites

    Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
    Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
    Ligand Binding and Linkage00:49

    Ligand Binding and Linkage

    Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
    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...
    Selectins01:25

    Selectins

    Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...