Identification, quantitation, and characterization of biomolecules by capillary electrophoretic analysis of binding interactions.
The high resolving power of capillary electrophoresis combined with the specificity of binding interactions may be used with advantage to characterize the structure-function relationship of biomolecules, to quantitate specific analytes in complex sample matrices, and to determine the purity of pharmaceutical and other molecules. We here review recent and innovative methodologies and applications of high resolution affinity electrophoresis within the fields of binding constant determination, structure-activity studies, quantitative microassays, analysis of drug purity and protein conformation, and immobilized affinity ligands. Despite the virtues of these approaches with respect to applicability, resolving power, speed, and low sample consumption, problems remain with respect to analyte identification and low concentration limits of detection. The ongoing development of new detector technologies for capillary electrophoresis such as mass spectrometry, and possibly nuclear magnetic resonance and other spectroscopic methods, is therefore very promising for the continued increased use of affinity capillary electrophoresis.
Heegaard
N H
NH
Department of Autoimmunology, Statens Serum Institut, Copenhagen, Denmark. nhe@ssi.dk
Kennedy
R T
RT
D001667:Binding, Competitive; D001685:Biological Factors / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D019075:Electrophoresis, Capillary / Q000379:methods*; D008024:Ligands; D015394:Molecular Structure; D004364:Pharmaceutical Preparations / Q000032:analysis; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
D001685:Biological Factors; D008024:Ligands; D004364:Pharmaceutical Preparations