Download PDF by P. Serra : Biosensors - Emerging Materials and Applications

By P. Serra

ISBN-10: 9533073284

ISBN-13: 9789533073286

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Wittmann, V. (2007). Probing multivalent carbohydrate-lectin interactions by an enzyme-linked lectin assay employing covalently immobilized carbohydrates. Bioorg. Med. 15, pp. 7661-7676. -K. & Whitesides, G. M. (1998). Polyvalent interactions in biological system: Implications for design and use of multivalent ligands and inhibitors. Angew. Chem. Int. 37, pp. 2754-2794. ; Dahmann, G. & Whitesides, G. M. (1995). Effective inhibitors of hemagglutination by influenza virus synthesized from polymers having active ester groups.

2005). Thermodynamic, kinetic, and electron microscopy studies of concanavalin A and Dioclea grandiflora lectin cross-linked with synthetic divalent carbohydrates. J. Biol. 280, pp. 8640-8646. ; Brewer, C. F. & Sacchettini, J. C. (1995). X-ray crystal structure of the soybean agglutinin cross-linked with a biantennary analog of the blood group I carbohydrate antigen. 34, pp. 4933-4942. Goldstein, I. J. & Poretz, R. D. (1986). in The Lectins: Liener, I. ; Sharon, N. & Goldstain, I. J. : Academic Press, Orlando, FL, pp.

2AB: red curves). The GST-C-SH2 and GST-N,C-(SH2)2 proteins gave minor responses with the pY515 ligand, while the free C-SH2 and N,C-(SH2)2 domains showed significant interaction (Fig. 2C-F: red curves). These results indicate that the GST part of these fusion proteins blocked the access to a pY515 interaction site, which became available for binding in the GST-free C-SH2 and N,C-(SH2)2 domains. Together, Figures 2C and 2D indicate that the CSH2 domain holds 2 different binding sites. One of these is accessible (C1-site) and the other is blocked (C2-site) in the GST-C-SH2 form.

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Biosensors - Emerging Materials and Applications by P. Serra

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