Electrophoretic Techniques (electrophoretic + techniques)

Distribution by Scientific Domains


Selected Abstracts


Liquid chromatography on chip

ELECTROPHORESIS, Issue 15 2010
Karine Faure
Abstract LC is one of the most powerful separation techniques as illustrated by its leading role in analytical sciences through both academic and industrial communities. Its implementation in microsystems appears to be crucial in the development of ,-Total Analysis System. If electrophoretic techniques have been widely used in miniaturized devices, LC has faced multiple challenges in the downsizing process. During the past 5 years, significant breakthroughs have been achieved in this research area, in both conception and use of LC on chip. This review emphasizes the development of novel stationary phases and their implementation in microchannels. Recent instrumental advances are also presented, highlighting the various driving forces (pressure, electrical field) that have been selected and their respective ranges of applications. [source]


Cover Picture: Electrophoresis 12/2008

ELECTROPHORESIS, Issue 12 2008
Article first published online: 23 JUN 200
This special issue on bioanalysis is aimed for compiling major trends in the development and application of electrophoretic techniques to the analysis of peptides, proteins, nucleic acids, carbohydrates and other biologically interesting compounds. This issue features a total of 30 contributions, containing six reviews and 23 original research articles. [source]


Separation of haemoglobin HbE and HbA2 by the fully automated, high-pressure liquid chromatography Tosoh HLC-723 G7 analyzer

INTERNATIONAL JOURNAL OF LABORATORY HEMATOLOGY, Issue 5 2008
G. LIPPI
Summary High-pressure liquid chromatography instruments specifically devised for separating haemoglobin (Hb) fractions have been increasingly employed by the hospital laboratories over the recent years since they allow easy and fast screening for several Hb variants. Although such instruments may be proposed as sensitive, specific and reliable alternatives to the classic electrophoretic techniques, a major drawback of this screening strategy is the almost identical retention time of several Hb variants. In particular, at least 18 Hb variants have been reported in the same retention window as HbA2, including HbE, the second most common ,-chain variant in humans after sickle cell trait. Recently, we evaluated the performance characteristics of an improved buffer formulation originally conceived for Hb variants separation procedures on the fully automated high-pressure liquid chromatography instrument Tosoh G7. At variance with other fully automated high-pressure liquid chromatography analyzers, the elution pattern on the G7 in subjects heterozygous for HbE is characterized by the presence of four suggestive peaks (HbF, HbA, HbA2 and HbE), confirming the effective separation of HbE from HbA2. Because of its potential value in the diagnosis of the thalassaemia syndromes, the effective separation of HbA2 from HbE can provide clinical laboratories with a valuable information for the diagnostic reasoning. [source]


Power and limitations of electrophoretic separations in proteomics strategies

MASS SPECTROMETRY REVIEWS, Issue 5 2009
Thierry Rabilloud
Abstract Proteomics can be defined as the large-scale analysis of proteins. Due to the complexity of biological systems, it is required to concatenate various separation techniques prior to mass spectrometry. These techniques, dealing with proteins or peptides, can rely on chromatography or electrophoresis. In this review, the electrophoretic techniques are under scrutiny. Their principles are recalled, and their applications for peptide and protein separations are presented and critically discussed. In addition, the features that are specific to gel electrophoresis and that interplay with mass spectrometry (i.e., protein detection after electrophoresis, and the process leading from a gel piece to a solution of peptides) are also discussed. © 2008 Wiley Periodicals, Inc., Mass Spec Rev 28:816,843, 2009 [source]


Analysis of glycosaminoglycan-derived disaccharides in biologic samples by capillary electrophoresis and protocol for sequencing glycosaminoglycans

BIOMEDICAL CHROMATOGRAPHY, Issue 2 2002
F. N. Lamari
Glycosaminoglycans are biologically significant carbohydrates which either as free chains (hyaluronan) or constituents of proteoglycans (chondroitin/dermatan sulfates, heparin, heparan sulfate and keratan sulfate) participate and regulate several cellular events and (patho)physiological processes. Capillary electrophoresis, due to its high resolving power and sensitivity, has been successfully used for the analysis of glycosaminoglycans. Determination of compositional characteristics, such as disaccharide sulfation pattern, is a useful prerequisite for elucidating the interactions of glycosaminoglycans with matrix effective molecules and, therefore, essential in understanding the biological functions of proteoglycans. The interest in the field of characterization of such biologically important carbohydrates is soaring and advances in this field will signal a new revolution in the area of glycomics equivalent to that of genomics and proteomics. This review focuses on the capillary electrophoresis methods used to determine the disaccharide pattern of glycosaminoglycans in various biologic samples as well as advances in the sequence analysis of glycosaminoglycans using both chromatographic and electrophoretic techniques. Copyright © 2002 John Wiley & Sons, Ltd. [source]