Cell surface glycans affinity

Incorporation of 9-AAz-NeuAc into cell surface glycans allows In situ photo-affinity crosslinking of CD22 to cis glycoprotein ligands... [Pg.9]

Incorporation of 9-BPC-NeuAc into cell surface glycans modulates CD22-ligand binding affinity in situ... [Pg.11]

The biotinylated glycans on the cell surfaces subsequently may be probed with (strept)avidin reagents to detect the azido-sialic acid modifications. Alternatively, the cells may be lysed and the glycoproteins isolated using an immobilized (strept)avidin or monomeric avidin affinity resin. [Pg.693]

Collins BE, Paulson JC. Cell surface biology mediated by low affinity multivalent protein-glycan interactions. Curr. Opin. Chem. Biol. 2004 8 617-625. [Pg.749]

Multi- and polyvalent interactions between lectins and glycans are of fundamental importance for the interaction of biological surfaces. Lectins are proteins with defined glycan-recognition domains on the surface of viruses and bacteria as well as of plant and animal cells. Affine inhibitors of lectins are, therefore, suitable for clarifying the function of defined carbohydrate stmctures, when they are used as a competitive binding partner. They also provide an opportunity for pharmacological intervention. The phenomenon of... [Pg.272]

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