Titlebook: Galectins; Methods and Protocol Sean R. Stowell,Connie M. Arthur,Richard D. Cummin Book 2022Latest edition Springer Science+Business Media,

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First Helicopters and Rotor Systemsonventional microscopy and enables reconstruction of virtual tridimensional images by acquiring multiple sections from several focal planes, which makes it possible to obtain the precise spatial location of any cellular structure or molecule. Furthermore, confocal microscopy is a non-invasive tissue

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Cloning, Expression, and Purification of Galectins for In Vitro Studies,on of GST-galectins from glutathione-conjugated Sepharose with excess glutathione is both efficient and innocuous. The ability to bind and elute GST-galectins from lactose-conjugated Sepharose with excess lactose provides a relatively easy means to insure that galectins are competent for glycoconjug

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,Introducing 77Se NMR Spectroscopy to Analyzing Galectin –Ligand Interaction,g. The documented strategic combination of synthetic carbohydrate chemistry and NMR spectroscopy prompts to envision to work with isotopically pure .Se-containing β-galactosides and to build on the gained experience with .Se by adding .F as second sensor in doubly labeled glycosides.

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Revealing the Identity of Human Galectin-3 as a Glycosaminoglycan-Binding Protein,they formed reversible noncovalent cross-linked complexes with the lectin. Binding of sulfated GAGs to Gal-3 was completely inhibited when Gal-3 was preincubated with β-lactose. Cross-linking of Gal-3 by CSA, CSC, and the bovine CSPG was also reversed by β-lactose. These findings strongly suggest th

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Mechanism of Mucin Recognition by Lectins : A Thermodynamic Study,bohydrate to carbohydrate epitope in these molecules leading to increased affinity. Importantly, the mechanism of binding of lectins to mucins appears similar to that for a variety of protein ligands binding to DNA. Recent results also show that high-affinity lectin–mucin cross-linking interactions

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Method for Identifying Galectin Ligands on Lymphocyte Membrane Glycoproteins,N-glycan structures on CD16a isolated from primary NK cells of healthy human donors was recently reported. NK cell CD16a is glycosylated at five N-glycosylation sites, and two of the five sites are modified, almost exclusively, by N-glycans with multiple LacNAc repeats which can serve as ligands for