Lectin-peroxidase Conjugate
Lectin-peroxidase Conjugate - Related Videos
20:23
A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
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Cited by 13 •
2009
Lectin-conjugated POROS beads were employed for HPLC. Glycopeptide standards served as positive and negative controls. MARS-14 depleted, trypsin-digested human plasma was chromatographed and flow-through (FT) and bound fractions collected for ESI-LC-MS/MS analyses. Glycopeptides were enriched in the bound fraction as compared to FT.
09:25
Lectin-based Isolation and Culture of Mouse Embryonic Motoneurons
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Cited by 21 •
2011
An alternative way of isolating mouse embryonic motoneurons from the spinal cord is described. The method takes into account the fact that lectin can bind to the low affinity nerve growth factor receptor p75NTR. This lectin-based preplating allows a purification similar to that with a specific antibody against the p75NTR.
08:11
Measuring Influenza Neuraminidase Inhibition Antibody Titers by Enzyme-linked Lectin Assay
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Cited by 54 •
2016
We describe the enzyme-linked lectin assay (ELLA) for measuring influenza neuraminidase (NA)-inhibition antibody titers in sera. The assay uses peanut agglutinin to quantify galactose residues that become accessible when NA removes sialic acid from fetuin-coated, 96-well plates.
02:50
Conjugated Proteins
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2020
Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties. Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
05:17
Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples
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Cited by 2 •
2016
This protocol describes the quick enrichment of leukocytes from small blood samples for a subsequent specific determination of the halogenating peroxidase activity within the cells. The method can be applied to human and non-human material and may contribute to the evaluation of new inflammatory markers.
FAQs
The two activities operate in sequence. The lectin first recognizes accessible carbohydrate structures on glycoproteins or glycolipids, establishing where the probe can bind. The attached peroxidase then converts an added substrate into a colored or otherwise measurable product. This coupling links molecular recognition to signal generation, allowing carbohydrate-containing targets to be localized or compared within an assay.
Signal interpretation depends on both glycan recognition and enzyme-generated detection. Different lectins can recognize different sugar residues, so the observed pattern reflects the carbohydrate structures recognized by the chosen probe rather than all surface glycans equally. Because the assay provides relative abundance information, results are best used to compare staining or signal patterns rather than assume a universal absolute glycan quantity.
Lectin-peroxidase conjugates and antibody-based assays answer related but different questions. A lectin probe reports the presence and distribution of recognized carbohydrate structures, whereas an antibody assay helps characterize particular molecular targets through antibody recognition. Using both approaches can connect glycan changes with specific host or pathogen molecules, strengthening interpretation of cell-surface or microbial-surface findings.
In a typical assay workflow, the conjugate is brought into contact with the sample so its lectin component can bind compatible carbohydrate structures. An added peroxidase substrate is then used to generate the detectable product. Researchers can examine the resulting color or other measurement to determine where recognized glycans occur and compare their relative signal across samples or regions.
For histochemical staining, the method helps visualize the distribution of carbohydrate-rich targets in a biological sample. In glycoprotein detection, the signal indicates locations containing lectin-recognized carbohydrate structures associated with those molecules. These applications are useful when the research question concerns spatial pattern or comparative abundance, because the readout can show where glycan-bearing material is concentrated.
In immunology and infection research, these conjugates can track glycan changes linked with immune activation, cell differentiation, or microbial infection. They also contribute to host-pathogen studies by revealing carbohydrate features on host or pathogen surfaces. Comparing patterns between conditions can identify changes in surface glycosylation and complement antibody-based evidence about the interaction.