Capillary Electrophoresis

University of Minnesota, Department of Chemistry, 207 Pleasant Street South East, Minneapolis, Minnesota 55455, United States.
Analytical Chemistry (Impact Factor: 5.83). 12/2011; 84(2):577-96. DOI: 10.1021/ac203205a
Source: PubMed

ABSTRACT Capillary Electrophoresis (CE) is a field that continues to grow. All areas of CE including theory, separation modes, instrumentation and applications remain highly active areas of research. This review includes a cross section of references from all areas of the field published in the two year period between Jan. 2010 and Nov. 2011. Web of Science reports over 4,000 articles, including 396 reviews, published with CE in the title, abstract or key words during this time period. Of these we have chosen 218 papers. We have attempted to choose papers that showcase some of the newest and most exciting developments in the field. It should be noted that papers describing electrophoresis in microfabricated devices were excluded since another review in this issue exclusively covers this topic.

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    • "We also performed qualitative and quantitative analysis of each of these compounds by two capillary electromigration methods: capillary zone electrophoresis (CZE) and micellar electrokinetic chromatography (MEKC). These two techniques are excellent tools for separation of both ionogenic and electroneutral compounds [23] [24] [25] and are frequently used for analysis and characterization of amino acids and their derivatives [26] [27] [28]. In addition, these DAP derivatives were characterized by their effective electrophoretic mobilities determined by CZE in acidic and alkaline classical or isoelectric background electrolytes (BGEs) or by MEKC in acidic and alkaline BGEs containing a micellar pseudostationary phase constituted by the anionic detergent sodium dodecyl sulfate (SDS) or the cationic detergent "
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    ABSTRACT: Thirteen mono-N-acyl derivatives of 2,6-diaminopimelic acid (DAP) - new potential inhibitors of the DapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase (DapE; EC were analyzed and characterized by IR and NMR spectroscopies and two capillary electromigration methods - zone electrophoresis (CZE) and micellar electrokinetic chromatography (MEKC). Structural features of DAP derivatives were characterized by IR and NMR spectroscopies whereas CZE and MEKC were applied to evaluate their purity and to investigate their electromigration properties. Effective electrophoretic mobilities of these compounds were determined by CZE in acidic and alkaline background electrolytes (BGEs) and by MEKC in acidic and alkaline BGEs containing a pseudostationary phase of anionic detergent sodium dodecylsulfate (SDS) or cationic detergent cetyltrimethylammonium bromide. The best separation of DAP derivatives, including diastereomers of some of them, was achieved by MEKC in an acidic BGE (500 mM acetic acid, pH 2.54, 60 mM SDS). All DAP derivatives were examined for their ability to inhibit catalytic activity of DapE from Haemophilus influenzae and ArgE from Escherichia coli. None of these DAP derivatives worked as an effective inhibitor of HiDapE but one derivative, N-fumaryl, Me-ester-DAP, was found to be moderate inhibitor of EcArgE, thus providing a promising lead structure for further studies on ArgE inhibitors.
    Analytical Biochemistry 09/2014; 467. DOI:10.1016/j.ab.2014.08.032 · 2.22 Impact Factor
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    • "CZE provides rapid and efficient separations of biological molecules [1] [2] [3]. CZE-ESI-MS/MS is an interesting tool for protein analysis [4]. "
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    ABSTRACT: We report the performance of capillary zone electrophoresis coupled with an electrokinetically pumped electrospray interface and an Orbitrap-Velos mass spectrometer for high sensitivity protein analysis. We first investigated the system for quantitation of the tryptic digest of BSA. The system produced outstanding linearity with respect to peak height, number of peptide IDs, and spectral counts across the range of 12 nM to 750 nM (60 amol to 3.5 fmol) of BSA injected. One peptide produced a detection limit of 0.3 nM (1.5 amol) injected. We also analyzed 700 pg of a tryptic digest prepared from a RAW264.7 cell lysate; ten proteins were identified in triplicate analyses after filtering the data with peptide confidence value as high. This sample size corresponds to the protein content of approximately ten eukaryotic cells.
    Proteomics 10/2012; 12(19-20):3013-9. DOI:10.1002/pmic.201200100 · 3.97 Impact Factor
  • Encyclopedia of Analytical Chemistry, 12/2010; , ISBN: 9780470027318
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