Recent advances in the application of capillary electrophoresis with mass spectrometric detection

Klampfl, Christian W.

doi:10.1002/elps.200500523

Cited by 116 publications

(86 citation statements)

References 199 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Among the variety of MS techniques used in combination with CE (for a comprehensive review see ref. [367]) the electrospray ionization (ESI) interface is the most conventional for integration with HPCE (for a review see ref. [368]).…”

Section: Electrospray Ionization Mass Spectrometry (Esi-ms) Detection-mentioning

confidence: 99%

Bioanalytical profile of the l-arginine/nitric oxide pathway and its evaluation by capillary electrophoresis

Boudko

2007

Journal of Chromatography B

View full text Add to dashboard Cite

This review briefly summarizes recent progress in fundamental understanding and analytical profiling of the L-arginine/nitric oxide (NO) pathway. It focuses on key analytical references of NO actions and on the experimental acquisition of these references in vivo, with capillary electrophoresis (CE) and high-performance capillary electrophoresis (HPCE) comprising one of the most flexible and technologically promising analytical platform for comprehensive high-resolution profiling of NO-related metabolites. Second aim of this review is to express demands and bridge efforts of experimental biologists, medical professionals and chemical analysis-oriented scientists who strive to understand evolution and physiological roles of NO and to develop analytical methods for use in biology and medicine.

show abstract

Section: Electrospray Ionization Mass Spectrometry (Esi-ms) Detection-mentioning

confidence: 99%

Bioanalytical profile of the l-arginine/nitric oxide pathway and its evaluation by capillary electrophoresis

Boudko

2007

Journal of Chromatography B

View full text Add to dashboard Cite

show abstract

“…CE is one of the techniques of choice for separation of the protein isoforms that are a result of microheterogeneity arising in the biosynthesis of a large number of proteins [1][2][3][4]. In CE, protein isoforms (e.g.…”

Section: Introductionmentioning

confidence: 99%

“…However, the use of second-order CE-DAD data for multiway analysis of individual protein isoforms is precluded because the UV spectra of the comigrating isoforms are indistinguishable from each other. In order to circumvent this problem, a detector with enhanced selectivity, such as a mass spectrometer [1][2][3][4], is necessary. To date, a few multiway data analysis methodologies have been described using CE-ESI-MS data [13,14], but to the best of our knowledge, none is related to the analysis of protein isoforms.…”

Section: Introductionmentioning

confidence: 99%

“…At low pH, the bound metal ions of MT sub-isoforms are released from the amino acid structures, giving rise to apothionein subisoforms. High-performance separations coupled to highresolution characterization techniques are key tools for clarifying the specific biological role of metallated and apo sub-isoforms, which is still unknown [1][2][3][4]8]. Furthermore, exploring multiway data analysis models for the study of the relatively simple CE-ESI-MS data sets obtained for the analysis of different MT samples constitutes an excellent benchmark for the study of proteins with a greater microheterogeneity.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

A multiway approach for classification and characterization of rabbit liver apothioneins by CE‐ESI‐MS

et al. 2008

View full text Add to dashboard Cite

We applied a multiway approach to extract information from the analysis of protein isoforms by CE-ESI-MS. Metallothioneins (MT) are low-molecular-weight proteins (6-7 kDa) with a strong affinity for heavy-metal ions. Rabbit liver MT-I and MT-II fractions are purified from MT samples. At low pH, the bound metal ions were released from the amino acid structures, giving rise to apothioneins. MT-I, MT-II and MT apothioneins, which are complex mixtures of protein isoforms, were analyzed by CE-ESI-MS. After data pre-processing, parallel factor analysis (PARAFAC) and multivariate curve resolution-alternating least squares (MCR-ALS) were applied to the data sets. In both cases, the models enabled classification of the protein samples and identification of their characteristic sub-isoforms using a set of three components. MCR-ALS required an initial estimate of the pure mass spectra of the three components. Thus, PARAFAC loadings were used to initialize the MCR-ALS optimization. The classifications obtained with MCR-ALS were slightly better than those obtained with PARAFAC, probably because MCR-ALS was less affected by the small migration time shifts of the preprocessed electropherograms. However, no differences were found between the pure mass spectra of the three components in either model. Finally, MCR-ALS allowed us to obtain an individual electrophoretic profile of each of the three components for each of the samples analyzed, which proved valuable for characterization and quantification purposes.

show abstract

“…Some examples of saccharidic compounds studied through CE combined with MS have been mentioned in recent reviews. In these works, examples of carbohydrates analysis are cited, together with many other applications, with the aim at showing the potential and recent advances of the CE-MS in a general perspective [25,26] or in specific fields [27][28][29][30].…”

Section: Introductionmentioning

confidence: 99%

Overview on advances in capillary electrophoresis‐mass spectrometry of carbohydrates: A tabulated review

et al. 2006

View full text Add to dashboard Cite

Overview on advances in capillary electrophoresis-mass spectrometry of carbohydrates: A tabulated reviewThe increasing interest for carbohydrates as holder of essential bioinformations has boosted their full characterization through analytical techniques. The intent of this review is to summarize the recent trends regarding on-line and off-line CE-MS coupling for carbohydrate analysis. A statistical survey on the articles that use derivatizing agents as well as on the analyzer and type of instrument coupling (i.e. on-or off-line) is depicted. From a general overview it can be concluded that, whereas derivatization might be useful for the detection of neutral carbohydrates improving separation selectivity with volatile buffers and increasing sensitivity of the MS detection, relatively few works with derivatized carbohydrates were found; this was noticed in particular for glycosides and saccharides carrying ionizable groups, which are normally analyzed without any chemical modification. The most applied coupling is the on-line sheath-liquid interface; for online applications, ESI is the sole source used, whilst the most common analyzer is the IT. MS n is often exploited, as fragmentation increases the achieved structural information. CE-MS turned out to be mainly used for the analysis of carbohydrates in drug development (i.e. study of oligosaccharides from pathogens, carbohydrate-based drugs and drug metabolites), in nutrition and for characterization of glycans from glycoproteins. The reader will find elucidating tables regarding these recent CE-MS applications, including the main information on the analysis conditions. Comments are meant to help the immediate focus on the usefulness of the analytical technique and predict the difficulties found during analysis and, in case, their overcoming.

show abstract

Recent advances in the application of capillary electrophoresis with mass spectrometric detection

Cited by 116 publications

References 199 publications

Bioanalytical profile of the l-arginine/nitric oxide pathway and its evaluation by capillary electrophoresis

Bioanalytical profile of the l-arginine/nitric oxide pathway and its evaluation by capillary electrophoresis

A multiway approach for classification and characterization of rabbit liver apothioneins by CE‐ESI‐MS

Overview on advances in capillary electrophoresis‐mass spectrometry of carbohydrates: A tabulated review

Contact Info

Product

Resources

About