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Affinity Capillary Electrophoresis to Examine Receptor-Ligand Interactions

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Capillary Electrophoresis of Proteins and Peptides

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 276))

Abstract

Afffinity capillary electrophoresis (ACE) is a new analytical technique that has been shown to be an efficient and accurate tool in studying biomolecular noncovalent interactions and determining binding and dissociation constants of formed complexes. ACE uses as its basis the change in migration time of a receptor upon binding to a ligand found in the electrophoresis buffer. Subsequent Scatchard analysis using noninteracting markers realizes a binding constant. Herein, ACE and three modifications in the technique, partial-filling ACE (PFACE), flowthrough PFACE (FTPFACE), and multiple-step ligand injection ACE (MSLIACE) are used to probe the binding of ristocetin A (Rist A) and vancomycin (Van) from Streptomyces orientalis to D-Ala-D-Ala terminus peptides and carbonic anhydrase B (CAB, E.C.4.2.1.1) to arylsulfonamides.

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© 2004 Humana Press Inc.

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Azad, M., Kaddis, J., Villareal, V., Hernandez, L., Silverio, C., Gomez, F.A. (2004). Affinity Capillary Electrophoresis to Examine Receptor-Ligand Interactions. In: Strege, M.A., Lagu, A.L. (eds) Capillary Electrophoresis of Proteins and Peptides. Methods in Molecular Biology™, vol 276. Humana Press. https://doi.org/10.1385/1-59259-798-X:153

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  • DOI: https://doi.org/10.1385/1-59259-798-X:153

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-58829-017-5

  • Online ISBN: 978-1-59259-798-7

  • eBook Packages: Springer Protocols

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