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Identification, quantitation, and characterization of biomolecules by capillary electrophoretic analysis of binding interactions
Author(s) -
Heegaard Niels H. H.,
Kennedy Robert T.
Publication year - 1999
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/(sici)1522-2683(19991001)20:15/16<3122::aid-elps3122>3.0.co;2-m
Subject(s) - capillary electrophoresis , analyte , biomolecule , affinity electrophoresis , chemistry , chromatography , electrophoresis , capillary electrophoresis–mass spectrometry , mass spectrometry , characterization (materials science) , small molecule , resolution (logic) , nanotechnology , affinity chromatography , biochemistry , electrospray ionization , materials science , computer science , artificial intelligence , enzyme
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.