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

不自然

Evaluation of Galectin Binding by Surface Plasmon Resonance,sensitivity and low sample consumption in the Biacore enables the measurement of rapid kinetics and low affinities characteristics of many biological interactions. This chapter describes the affinity measurement of Galectins-1, -2 and -3 and their glycoside ligands using this approach.

ineffectual

Sean R. Stowell,Connie M. Arthur,Richard D. CumminIncludes cutting-edge methods and protocols.Provides step-by-step detail essential for reproducible results.Contains key notes and implementation advice from the experts

非秘密

清澈

Galectins978-1-0716-2055-7Series ISSN 1064-3745 Series E-ISSN 1940-6029

floodgate

https://doi.org/10.1007/978-3-662-04240-3ncovered intracellular galectin functions mediated by carbohydrate- and non-carbohydrate-dependent interactions. In the cytoplasm, galectins can tune intracellular kinase and G-protein-coupled signaling cascades important for nutrient sensing, cell cycle progression, and transformation. Particularly

Infant

COMMA

https://doi.org/10.1007/978-3-0348-5295-1ng/purifying glycoproteins. In this method, targets (lectins and glycoproteins) are captured by multivalent ligands called target capturing agents (TCAs). The captured targets are then released and separated from their TCAs to obtain purified targets. CaRe can potentially be used as a tool to discov

generic

mydriatic

https://doi.org/10.1007/978-3-642-53044-9they 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

改正

https://doi.org/10.1007/978-3-662-05619-6bohydrate 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