Titlebook: Lectins and Glycobiology; Hans-Joachim Gabius,Sigrun Gabius Book 1993 Springer-Verlag Berlin Heidelberg 1993 Adh?sion.Biosignalübertragung

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Determination of Carbohydrate Specificity in Solid-Phase Assaystides (or glycoproteins) to inhibit lectin-mediated hemagglutination or glycoconjugate precipitation. These methods require relatively large quantities of glycoconjugates which can be difficult to obtain in sufficient quantities for inhibition studies. Suitable ligands for agglutination may only be

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Chemical Modification of Lectins by Group-Specific Reagentsr labeling reagents without adversely affecting the ligand-binding properties. When modification is carried out in the absence or presence of a suitable ligand, any differential effect hints at the involvement of certain groups in ligand binding. Impairment of ligand binding only in the absence of t

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Study of Oligosaccharide-Lectin Interaction by Various Nuclear Magnetic Resonance (NMR) Techniques af biomolecules in solution. These powerful methods are necessary if one wants to study and understand biomolecular interaction processes on an atomic level. In this chapter we introduce methods which are suitable for a study of lectin-oligosaccharide interaction on this level. The first step is assi

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Lectin-Glycoconjugate Cross-Linking Interactionslycolipids which, in many cases, is associated with a variety of biological responses. For example, cross-linking of glycoconjugates on the surface of cells has been implicated in the mitogenic activities of lectins such as Concanavalin A (Con A) and soybean agglutinin (SBA) (cf. Nicolson 1976); in

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Glycoprotein-Lectin-Immunosorbent Assay (GLIA)lycosylation of proteins and lipids. (Schachter 1984; Martinez and Barsigian 1987). The structural analysis of the glycans of single purified glycoproteins requires, however, a range of extraordinarily complicated and costly methods. For this reason, the investigation of changes in protein glycosyla

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Determination of Carbohydrate Specificity in Solid-Phase Assaysrated from unbound lectin is one practical approach (see Allen et al. chapter 7 of this Vol.). Moreover, a lectin is immobilized onto a nitrocellulose membrane by spotting or an ELISA plate surface by adsorption, the immobilized lectin then specifically interacts with labeled (e.g., biotinylated) li