Separations by Continuous Electrochromatography

Karler, Arthur

doi:10.1021/ac60149a035

Cited by 88 publications

(15 citation statements)

References 15 publications

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“…Crystalline warfarin sodium was added to pooled normal human plasma to achieve a concentration of 200 mg per ml. The plasma-warfarin mixture was fed to a continuous flow electrophoretic apparatus at a rate of 1.4 ml per hour (2). It was applied to the top of the curtain about one-third of the distance from the cathode toward the anode.…”

Section: Methodsmentioning

confidence: 99%

Studies on the Coumarin Anticoagulant Drugs: Interaction of Human Plasma Albumin and Warfarin Sodium*

O’Reilly¹

1967

J. Clin. Invest.

110

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Summary. In studies by continuous flow electrophoresis the coumarin anticoagulant drug warfarin sodium was found to be bound solely to the albumin fraction of the plasma proteins. The interaction was studied in detail by equilibrium dialysis of solutions of crystalline human plasma albumin and warfarin sodium. Analysis of the data showed that albumin possesses a single strong binding site for warfarin with an association constant of 154,-000 at 30 C and secondary classes of several sites with a much lower affinity. The free energy of binding for the first anion determined at 3°and 370 C was -6.54 and -7.01 kcal per mole, respectively. The standard enthalpy change for the interaction was -3.48 kcal per mole, and the entropy change was +11.2 U.The negative enthalpy change was surprisingly large and the positive entropy change small for an anion-albumin interaction, suggesting significant nonionic binding. The inability to saturate the albumin binding sites, even when high concentrations of warfarin were used, is consistent with a reversible configurational alteration of the albumin molecule during the binding process. The thermodynamic data indicate that the albumin binding sites for warfarin sodium are formed during the process of binding, rather than being preformed as in antigen-antibody reactions. The strength of the binding process suggests that many of the pharmacodynamic characteristics of warfarin sodium in man are determined by its strong interaction with plasma albumin. Such correlations of the physicochemical interactions and biologic effects of the coumarin anticoagulant drugs should lead to a better understanding of their mechanisms of action.

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Section: Methodsmentioning

confidence: 99%

Studies on the Coumarin Anticoagulant Drugs: Interaction of Human Plasma Albumin and Warfarin Sodium*

O’Reilly¹

1967

J. Clin. Invest.

110

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“…Under these conditions (which are particularly likely to be encountered in exploratory strip runs) this factor is very much further from unity in Eq. [6] than in Eq. [5].…”

Section: + K~[z]mentioning

confidence: 99%

“…We have to investigate the following simultaneous equilibria, for which the constants are given: [5] [6] constant for the first (exchange) reaction is the original assumption of light loading. Under these conditions we may neglect the competing ion (dimethylammonium in the present case).…”

Section: + K~[z]mentioning

confidence: 99%

“…In Eq. [6] the resin affinity factor K%/K% (which relates essentially to chromatographic phenomena) has not disappeared, a result arising wholly as a consequence of the mobility of sorbed ions within the solid phase. In general, for a series of like ions, the greater the mobility of an ion the greater is its affinity for an ion-exchange resin and the lower the stability of its complexes (20,24).…”

Section: [M]~mentioning

confidence: 99%

“…The basis of the comparison will then be Eq. [ 5] and [6]. But the most straightforward experimental technique is It rises to a limiting value---the inverse ratio of formation constants.…”

Section: Use Of Resins Of Low Ionic Specificity--the Abovementioning

confidence: 99%

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Continuous Electrochromatography on Ion-Exchange Membranes

Caplon

1961

J. Electrochem. Soc.

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It is shown theoretically that in continuous electrochromatography the use of an ion-exchange resin can lead to improved separations. This is because a stationary phase capable of highly selective sorption is provided, within which ions are immobilized with respect to eluant flow but not with respect to current flow. In a system of this kind, in contrast with systems employing conventional supporting media, synergy arises between electrophoresis and chromatography. Even if the ions undergoing separation do not differ greatly in their affinities for the resin, certain advantages result from its presence, particularly when the eluant contains a complexing agent.

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A New Low Cost, Fully Automated Amino Acid Analyzer Using a Gradient HPLC

Klapper

1982

Methods in Protein Sequence Analysis

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Separations by Continuous Electrochromatography

Cited by 88 publications

References 15 publications

Studies on the Coumarin Anticoagulant Drugs: Interaction of Human Plasma Albumin and Warfarin Sodium*

Studies on the Coumarin Anticoagulant Drugs: Interaction of Human Plasma Albumin and Warfarin Sodium*

Continuous Electrochromatography on Ion-Exchange Membranes

A New Low Cost, Fully Automated Amino Acid Analyzer Using a Gradient HPLC

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