@article {2271,
	title = {Behavior of interacting species in vacancy affinity capillary electrophoresis described by mass balance equation},
	journal = {Electrophoresis},
	volume = {29},
	number = {16},
	year = {2008},
	note = {ISI Document Delivery No.: 343MCTimes Cited: 0Cited Reference Count: 42Sun, Ying Fang, Ning Chen, David D. Y.},
	month = {Aug},
	pages = {3333-3341},
	type = {Article},
	abstract = {Vacancy ACE (VACE) is one of the ACE methods, and has been used to study binding interactions between different biomolecules. Thermodynamic binding constants can be estimated with nonlinear regression methods. With a highly efficient computer simulation program (SimDCCE), it is possible to demonstrate the detailed behaviors of each species during the interaction process under different conditions. In this work, thirteen scenarios in four different combinations of migration orders of the free protein, free drug, and complex formed are studied. The detailed interaction process between protein and ligand is discussed and illustrated based on the mass balance equation, also called mass transfer equation. By properly setting the parameters in the simulation model, the influence of different factors during the interaction process can be well understood.},
	keywords = {affinity capillary electrophoresis, binding constant, COMPUTER-SIMULATION, CONSTANTS, DRUG-PROTEIN-BINDING, equation, EXPERIMENTAL VALIDATION, FRONTAL ANALYSIS, HUMAN-SERUM-ALBUMIN, HUMMEL-DREYER, mass balance, method, PERFORMANCE LIQUID-CHROMATOGRAPHY, vacancy affinity capillary electrophoresis, WALL ADSORPTION, ZONE-ELECTROPHORESIS},
	isbn = {0173-0835},
	url = {<Go to ISI>://000258856900008},
	author = {Sun, Y. and Fang, N. and Chen, D. D. Y.}
}
@article {397,
	title = {Applications of on-line weak affinity interactions in free solution capillary electrophoresis},
	journal = {Electrophoresis},
	volume = {23},
	number = {6},
	year = {2002},
	note = {ISI Document Delivery No.: 536KNTimes Cited: 26Cited Reference Count: 109},
	month = {Mar},
	pages = {815-822},
	type = {Review},
	abstract = {The impressive selectivity offered by capillary electrophoresis can in some cases be further increased when ligands or additives that engage in weak affinity interactions with one or more of the separated analytes are added to the electrophoresis buffer. This on-line affinity capillary electrophoresis approach is feasible when the migration of complexed molecules is different from the migration of free molecules and when separation conditions are nondenaturing. In this review, we focus on applying weak interactions as tools to enhance the separation of closely related molecules, e.g., drug enantiomers and on using capillary electrophoresis to characterize such interactions quantitatively. We describe the equations for binding isotherms, illustrate how selectivity can be manipulated by varying the additive concentrations, and show how the methods may be used to estimate binding constants. On-line affinity capillary electrophoresis methods are especially valuable for enantiomeric separations and for functional characterization of the contents of biological samples that are only available in minute quantities.},
	keywords = {affinity capillary electrophoresis, ALPHA(1)-ACID, AMYLOID-P COMPONENT, biomolecular interactions, capillary electrophoresis, CHIRAL SEPARATION, CHROMATOGRAPHY, CONSTANTS, ELECTROKINETIC, enantiomer separation, ENANTIOSELECTIVE PROTEIN, FRONTAL ANALYSIS, GLYCOPROTEIN, isotherms, MEASURE BINDING, PARTIAL-FILLING TECHNIQUE, PROTEIN-BINDING, review, separation methods, ZONE-ELECTROPHORESIS},
	isbn = {0173-0835},
	url = {<Go to ISI>://000174699400002},
	author = {Heegaard, N. H. H. and Nissen, M. H. and Chen, D. D. Y.}
}
