Recent developments in capillary zone electrophoresis of proteins

Dolnı́k, Vladislav

doi:10.1002/(sici)1522-2683(19991001)20:15/16<3106::aid-elps3106>3.0.co;2-2

Cited by 55 publications

(32 citation statements)

References 123 publications

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“…Most CIEF peaks in Fig. 3, including the narrowest peaks (peaks [16][17][18][19][20][21][22], are reproducibly observed. For other peaks (e.g., peaks 10-12 and 15), some minor differences in peak resolution and intensity are evident.…”

Section: Cief Of Protein Complexesmentioning

confidence: 79%

“…Our previous comparison between CZE and gradient capillary reversed-phase liquid chromatography (RPLC) in the separation of tryptic digests of yeast lysate showed that CZE yielded a lower resolution than the RPLC approach [37]. Similarly, CZE of proteins is limited to separations of less complex mixtures [17,18,20]. For complex proteomic samples, CZE is best utilized as the second dimension in two-dimensional separations because of its speed and relatively high efficiency in the "isocratic elution" mode (see Section 4; Multidimensional separations).…”

Section: Czementioning

confidence: 99%

“…Liquid-phase separations, often within capillaries, are increasingly recognized as the best separations technique for this approach. Developments in capillary electrophoresis applicable to separating peptides and proteins have been reviewed in several Electrophoresis publications [16][17][18][19][20].…”

Section: Introductionmentioning

confidence: 99%

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Proteomics based on high-efficiency capillary separations

2002

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Identifying and quantifying in a high throughput manner the proteins expressed by cells, tissues or an organism provides the basis for understanding the functions of its constituents at a "systems" level. As a result, proteome analysis has increasingly become the focus of significant interest and research over the past decade. This is especially true following the recent stunning achievements in genomics analyses. However, unlike the static genome, the complexities and dynamism of the proteome present significant analytical challenges and demand highly efficient separations and detection technologies. A number of recent technological advancements have been in direct response to these challenges. Currently, strategically mated combinations of sophisticated separations techniques and advanced mass spectrometric detection represent the best approach to addressing the intricacies of the proteome. Liquid-phase separations, often within capillaries, are increasingly recognized as the best separations technique for this approach. In combination on-line with mass spectrometry, liquid-phase separations provide the improved analytical sensitivity, sample throughput, and quantitation capabilities necessitated by the multifaceted problems within proteomics analyses. This review focuses primarily on current high-efficiency capillary separations techniques, including both capillary liquid chromatography and capillary electrophoresis, applied to the analysis of complex proteomic samples. We emphasize developments at our laboratory and illustrate technical advances that attempt to review the role of separations within the broader context of a state-of-the-art integrated proteomics effort.

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Section: Cief Of Protein Complexesmentioning

confidence: 79%

Section: Czementioning

confidence: 99%

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Proteomics based on high-efficiency capillary separations

2002

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“…Previously, we have reviewed the use of CE for the analysis of proteins for the periods of 1992-1997 [1], 1997-1999 [2], 1999-2001 [3], and 2001-2003 [4]. This review particularly emphasizes practical applications of CE, but also includes sections on technique and theory, including modeling migration of proteins and CE systems, sample preparation, coatings, improving separation, detection, and use of various modes of CE.…”

Section: Introductionmentioning

confidence: 99%

Capillary electrophoresis of proteins 2003–2005

Dolnı́k¹

2006

Electrophoresis

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139

117

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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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“…[1][2][3][4][5][6][7][8][9][10][11][12][13][14] By building on these and earlier efforts, it is anticipated that the popularity of CE-MS will grow, and its advantages will be better appreciated and exploited.…”

Section: Introductionmentioning

confidence: 99%

Recent Developments in Capillary Electrophoresis–Mass Spectrometry of Proteins and Peptides

Monton

Terabe

2005

ANAL. SCI.

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Many researchers have invested considerable efforts toward improving capillary electrophoresis (CE)-mass spectrometry (MS) systems so they can be applied better to standard analyses. This review highlights the developments in CE-MS of proteins and peptides over the last five years. It includes the developments in interfaces, sample-enrichment techniques, microfabricated devices, and some applications, largely in capillary zone electrophoresis (CZE), capillary isoelectric focusing (CIEF) and capillary isotachophoresis formats.

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Recent developments in capillary zone electrophoresis of proteins

Cited by 55 publications

References 123 publications

Proteomics based on high-efficiency capillary separations

Proteomics based on high-efficiency capillary separations

Capillary electrophoresis of proteins 2003–2005

Recent Developments in Capillary Electrophoresis–Mass Spectrometry of Proteins and Peptides

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