Capillary Electrophoresis of Proteins 2003–2005

Alcor BioSeparations, Santa Clara, CA, USA.
Electrophoresis (Impact Factor: 3.03). 01/2006; 27(1):126-41. DOI: 10.1002/elps.200500567
Source: PubMed


This review article with 304 references describes recent developments in CE of proteins, and covers the two years since the previous review (Hutterer, K., Dolník, V., Electrophoresis 2003, 24, 3998-4012) through Spring 2005. It covers topics related to CE of proteins, including modeling of the electrophoretic migration of proteins, sample pretreatment, wall coatings, improving separation, various forms of detection, special electrophoretic techniques such as affinity CE, CIEF, and applications of CE to the analysis of proteins in real-world samples including human body fluids, food and agricultural samples, protein pharmaceuticals, and recombinant protein preparations.

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Available from: Vlad Dolnik, Jun 27, 2014
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    • "Nowadays, electrophoretic separation methods are widely applied to study polyelectrolytes (PEs) such as proteins, DNA and synthetic polymers [1] [2] [3]. While there exist several theories [4] [5] [6] [7] that have been successfully used to describe qualitatively the experimentally observed behaviour of various PEs, there are still many open problems to address. "
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    ABSTRACT: The effect of hydrodynamic interactions on the free-solution electrophoresis of polyelectrolytes is investigated with coarse-grained molecular dynamics simulations. By comparing the results to simulations with switched-off hydrodynamic interactions, we demonstrate their importance in modelling the experimentally observed behaviour. In order to quantify the hydrodynamic interactions between the polyelectrolyte and the solution, we present a novel way to estimate its effective charge. We obtain an effective friction that is different from the hydrodynamic friction obtained from diffusion measurements. This effective friction is used to explain the constant electrophoretic mobility for longer chains. To further emphasize the importance of hydrodynamic interactions, we apply the model to end-labelled free-solution electrophoresis.
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    ABSTRACT: Cereal grains are widely used for human food and animal feed throughout the world. Distinction between the various genotypes of any cereal species is important to segregate grains according to utilization type. DNA analysis indicates genotype (variety), whereas protein composition provides information about both variety and likely processing properties, reflecting the contributions of both genotype and growth/storage conditions. Standard methods of protein and DNA analysis involve gel electrophoresis in various formats. Capillary electrophoresis (CE) is one of the newer techniques to be so used. CE is a valuable addition to other methods of cereal protein and DNA analysis and should, in time, be applicable to analyzing DNA and all protein classes from all cereal grains. This review focuses on methods for distinguishing genotypes based on th e protein and DNA composition of the grain by capillary electrophoresis. Microfluidic capillary electrophoresis (Lab-on-a-chip), a newly advanced and rapid technique, is also discussed.
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    ABSTRACT: Proteome analysis is now emerging as key technology for deciphering biological processes and the discovery of biomarkers for diseases from tissues and body fluids. The complexity and wide dynamic range of protein expression poses a formidable challenge to both peptide separation technologies and mass spectrometry (MS). Here we review the efforts that have been undertaken to date, focussing on capillary electrophoresis coupled to mass spectrometry (CE-MS). We discuss CE-MS from an application point of view evaluating its merits and vices in regard to biomarker discovery and clinical applications. As examples, we present the use of CE-MS for the determination of protein patterns in urine, serum, and other body fluids. Finally, the benefits and limitations of CE-MS for the analysis of proteins in clinical samples are discussed against the background of alternative technologies.
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