AI Article Synopsis
- - Fluorescently labeled (strept)avidins are commonly used to detect biotinylated molecules in immunology and histochemistry, but they can also bind to various glycans, including components of blood group antigens and other oligosaccharides.
- - This binding occurs in a dose-dependent manner, meaning that the presence of certain polymeric glycan conjugates can inhibit this interaction, but monomeric forms do not have the same effect.
- - The ability of (strept)avidins to bind glycans may lead to inaccuracies in carbohydrate sample analysis, suggesting that researchers should avoid using excessive amounts of (strept)avidin in their experiments to minimize these errors.
Article Abstract
Fluorescently labeled and conjugated (strept)avidins are widely used for imaging biotinylated molecules in immunological assays and histochemistry. We showed that besides biotin, these proteins bind glycans, including fragments of mammalian glycoproteins and glycolipids, in particular, ABO blood group antigens, oligolactosamines, and 6--sulfated oligosaccharides. This interaction is inhibited in a dose-dependent manner by micromolar concentrations of polymeric, but not monomeric, glycan conjugates (i.e., requires polyvalence). Taking into account the cluster organization of cell glycans (glycoproteins and glycolipids), the ability of (strept)avidins to bind glycans might be a source of errors in the analysis of carbohydrate-containing samples, which can be prevented by avoiding a large excess of (strept)avidin in analytical systems.
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| http://dx.doi.org/10.1134/S0006297924110142 | DOI Listing |
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