Phaseolus Vulgaris Lectin
Phaseolus Vulgaris Lectin - Related Videos
10:26
The Infiltration-centrifugation Technique for Extraction of Apoplastic Fluid from Plant Leaves Using Phaseolus vulgaris as an Example
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Cited by 100 •
2014
This protocol details the optimized extraction of apoplast washing fluid from plant leaves, using French bean plants (Phaseolus vulgaris) as a model example.
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.
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.
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.
10:25
In Utero Intra-cardiac Tomato-lectin Injections on Mouse Embryos to Gauge Renal Blood Flow
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Cited by 2 •
2015
This manuscript describes a technique for visualization of the developing vasculature. Here we utilized in utero intra-cardiac FITC-labeled tomato lectin microinjections on mouse embryos. Using this technique, we delineate the perfused and unperfused vessels throughout the embryonic kidney.
FAQs
Its multiple binding sites can attach to carbohydrate structures on separate neighboring cells or cellular components. A single lectin molecule may therefore act as a bridge, producing cross-linking rather than isolated binding. When the interactions are sufficiently extensive and occur under suitable conditions, the linked cells form visible aggregates, providing a biological readout of surface carbohydrate organization.
Binding depends on the identity and arrangement of sugar structures displayed on a cell surface or other cellular component. Differences in these glycans can change whether attachment occurs and how extensively molecules become cross-linked. Researchers can use that selectivity to compare carbohydrate patterns and connect molecular recognition with differences in cell interactions or cellular responses.
Binding describes attachment between the lectin and a recognized carbohydrate structure, whereas agglutination requires enough attachments to link multiple cells or cellular components together. Thus, detectable molecular recognition does not necessarily produce aggregation. Keeping these outcomes separate helps researchers interpret whether an experiment demonstrates surface recognition alone or broader consequences of multivalent cross-linking.
Carbohydrates associated with receptors can provide more than passive attachment sites. When the lectin engages these structures, the interaction may influence receptor-linked cellular responses, depending on the biological context and conditions. This makes the protein useful for examining how cell-surface glycans participate in signaling-related effects, rather than treating carbohydrates only as surface markers.
A study can first select cells or cellular components whose surface carbohydrates are relevant to the question. Researchers then examine lectin attachment and, where appropriate, monitor cross-linking or agglutination. They may also assess associated cellular responses. This workflow connects carbohydrate recognition with observable changes in cell interactions and supports comparative glycobiology experiments.
Lectin interactions can help characterize which carbohydrate features are displayed on cells or cellular components and how those features support molecular attachment. Patterns of binding or aggregation provide information about surface glycan organization and accessibility. In glycobiology and cell biology, these observations help relate carbohydrate composition to interactions between cells and their surroundings.
The protein connects molecular glycobiology with the biology of common beans in two ways. It supports investigation of plant defense proteins and also helps examine biological consequences associated with consuming inadequately processed beans. This context broadens its importance beyond laboratory cell studies, linking carbohydrate-binding activity to plant biology and food-related biological effects.