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Affinity Capillary Electrophoresis in Pharmaceutics and by Reinhard H. H. Neubert, Hans-Hermann Ruttinger

By Reinhard H. H. Neubert, Hans-Hermann Ruttinger

The authors supply techniques to discover and represent interactions among medications, drug cars, and organic membranes to facilitate advancements in managed drug supply and focusing on. The ebook comprises present purposes and methods to spot binding constants among medicines, organic constructions, proteins, nucleic acids, and plasmids, raise drug bioavailability, improve the permeability, solubility, energy, and serve as of drug formulations, learn protein-protein exchanges and reactions, and calculate pKa values.

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Extra info for Affinity Capillary Electrophoresis in Pharmaceutics and Biopharmaceutics

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The use of organic solvents in nonaqueous capillary electrophoresis not only increases the solubility of the solutes, but also allows one to control important characteristics of the separation. For instance, the solvent properties affect the acid–base behavior of the analytes on a wider scale than © 2003 by Marcel Dekker, Inc. possible in water. The pKa values can differ up to many orders of magnitude. Hence, electrophoretic mobilities can be controlled efficiently, and separations not possible in aqueous CE can be performed with excellent selectivities (11).

Micellar electrokinetic chromatography is applied for the analysis of a wide variety of organic substances, ionic and nonionic in nature. For instance, for the determination of the content of active pharmaceutical ingredients in tablets, creams, and injectables, the MEKC mode often offers advantages over the CZE mode. © 2003 by Marcel Dekker, Inc. D. Capillary Electrochromatography Capillary electrochromatography is very similar to MEKC. It is a technique where the flow of the mobile phase through a column packed with an HPLC stationary phase is effected by the application of an external voltage.

Since only viscosity ratios have to be determined, only the traveling-time ratios have to be considered, provided that all measurements are done with the same capillary at constant pressure. Evaluation of experimental data is much easier when Eq. (14) is converted to a linear form. There are three linearizations established in practice: Double reciprocal plot (Benesi–Hildebrand or Lineweaver–Burk): 1 1 1 1 = и ϩ ␮ Ϫ ␮S ( ␮SL Ϫ ␮S )иKA [L] ␮SL Ϫ ␮S (18) Y-reciprocal plot: [L] 1 1 = и[L] ϩ ␮ Ϫ ␮S ␮SL Ϫ ␮S (␮SL Ϫ ␮S )иKA (19) X-reciprocal plot (Scatchard or Eadie): ␮ Ϫ ␮S = ϪKA и(␮ Ϫ ␮S ) ϩ KA и(␮SL Ϫ ␮S ) [L] (20) The names of the linearization methods correspond to the established methods in protein affinity research and alternatively in enzymology.

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