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  • 1
    Electronic Resource
    Electronic Resource
    Sensitivity enhancement and second-dimensional information from solid phase extraction-capillary electrophoresis of entire high-performance liquid chromatography fractions (1995)
    Weinheim : Wiley-Blackwell
    Electrophoresis 16 (1995), S. 541-548 
    Details
    ISSN: 0173-0835
    Keywords: Solid phase extraction-capillary electrophoresis ; On-line sample concentration ; Solid phase ; Peptides ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A novel separation technique is demonstrated for peptide analysis of entire 100 μL high-performance liquid chromatography (HPLC) fractions in a single, low pH, capillary zone electrophoresis (CZE) separation. The method employs a hybrid capillary consisting of a removable inlet section containing a reverse-phase packing and a standard CZE bare-fused silica separation capillary. The packed tip allows sample to be concentrated at flow rates greater than 20 μL/min and released in a controlled manner for CZE separation. Separations are comparable to standard CZE with minor modifications in selectivity. Using a mixture of model peptides, the hybrid capillary is shown to effect enhancement in sensitivity of ≥ 100-fold. Five fractions from the HPLC separation of peptides obtained from the digestion of bovine serum albumin (BSA) were analyzed by the solid phase extraction-capillary electrophoresis (SPE-CE) method which was shown to provide rapid second-dimensional information. Practical concentration limits of detection for peptides are calculated to be 1--10 ng/mL with this technology.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150160189
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  • 2
    Electronic Resource
    Electronic Resource
    Evaluation of capillary electrophoresis in polymer solutions with laser-induced fluorescence detection for the automated detection of T-cell gene rearrangements in lymphoproliferative disorders (1996)
    Weinheim : Wiley-Blackwell
    Electrophoresis 17 (1996), S. 1491-1498 
    Details
    ISSN: 0173-0835
    Keywords: Capillary electrophoresis ; Polymer solutions ; Polymerase chain reaction ; T-cell receptor (TCRγ) ; Gene rearrangements ; Laser-induced fluorescence ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The rapid increase in the number of DNA-based clinical diagnostic procedures, particularly polymerase chain reaction (PCR)-based assays, has generated interest in analytical techniques that are less time-consuming and labor-intensive than traditional procedures such as polyacrylamide gel electrophoresis (PAGE). Capillary electrophoresis with laser-induced fluorescence (CE-LIF) detection, which allows for rapid and sensitive detection of DNA fragments in an automated format, is well-suited for DNA-based clinical assays. In this study, we demonstrate the potential of CE-LIF for the detection of PCR products from T-cell receptor gamma (TCRγ) gene rearrangements present in monoclonal populations of lymphocytes. The presence of monoclonal populations of T-cells is associated (but not always synonymous) with lymphocytic malignancies. Analysis of 31 patient samples, as well as sensitivity controls, demonstrated that CE-LIF detection of monoclonal lymphocytic populations is comparable to that of PAGE-SYBR Green I staining, and that CE-LIF detection can be accomplished in less than 20 min. These preliminary results illustrate the potential feasibility of a CE-based diagnostic assay for the detection of T-cell gene rearrangements.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150170914
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  • 3
    Electronic Resource
    Electronic Resource
    Editorial (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 1707-1708 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150181002
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  • 4
    Electronic Resource
    Electronic Resource
    Capillary electrophoresis as a clinical tool for the analysis of protein in serum and other body fluids (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 1715-1723 
    Details
    ISSN: 0173-0835
    Keywords: Clinical analysis ; Protein ; Capillary electrophoresis ; Serum ; Hemoglobin ; Immunoglobulin ; Isozymes ; Lipoprotein ; Glycoprotein ; Transferrin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Most electrophoretic analyses of proteins in the clinical laboratory are currently carried out by electrophoresis in acrylamide or agarose gels. This labor-intensive method is now being challenged by capillary electrophoresis (CE) because of its potential for automated, rapid, high efficiency separations. The automatability of CE itself, combined with its amenability to interfacing with other robotized functions, positions this technology perfectly for the analysis of proteins in physiological matrices, such as serum, urine, and cerebrospinal fluid. The focus of this overview is to familiarize the clinical scientist with the research demonstrating the applicability of the technology to the clinical protein laboratory.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150181004
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  • 5
    Electronic Resource
    Electronic Resource
    Effect of cationic buffer additives on the capillary electrophoretic separation of serum transferrin from different species (1996)
    Weinheim : Wiley-Blackwell
    Electrophoresis 17 (1996), S. 431-437 
    Details
    ISSN: 0173-0835
    Keywords: Capillary electrophoresis ; Carbohydrate-deficient transferrin ; Transferrin ; Sialic acid ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The presence of specific transferrin (Tf) glycoforms in human serum has been shown to correlate with certain clinical syndromes. Hence, the ability to separate and quantitatively measure the various forms of human transferrin has become increasingly important. As a means of evaluating the potential for developing a rapid capillary electrophoresis-based assay for the analysis of carbohydrate-deficient transferrins (CDTs), the capillary zone electrophoretic (CZE) analysis of Tfs from several species was evaluated using uncoated capillaries and a separation augmented with cationic additives. With bovine Tf, five peaks (representing different sialylated forms) were partially resolved in borate and baseline-resolved when 1,4-diaminobutane was added to the buffer. These same conditions were found to be inadequate for the resolution of the sialo-forms from other species. Some success was achieved using α,γ-bis-quaternary ammonium alkanes instead of the 1,4-diaminobutane and optimizing the pH for each of the species Tfs. Human Tf was found to be resolved in an uncoated capillary equilibrated with a borate buffer containing millimolar concentrations of decamethonium bromide as a buffer additive. Under these conditions, resolution of the various sialoforms from the iron-saturated Tf was possible and the glycoforms were found to migrate differently than their iron-depleted counterparts. Despite the resolution achievable under these conditions, the lengthy analysis time is incompatible with the requirements for a clinical CZE-based assay.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150170224
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  • 6
    Electronic Resource
    Electronic Resource
    Hydrophobic peptide mapping of clinically relevant heptathelical membrane proteins by capillary electrophoresis (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 1767-1774 
    Details
    ISSN: 0173-0835
    Keywords: Capillary electrophoresis ; Bacteriorhodopsin ; Hydrophobic peptide mapping ; Solid-phase extraction ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The structural investigation of G protein-coupled receptors has been hindered by the lack of techniques to effectively resolve the hydrophobic peptides obtained by chemical or proteolytic cleavage, as well as the minute amounts of protein typically isolated. We have developed a capillary electrophoresis method for efficient separation of hydrophobic peptides using a cyanogen bromide digest of bacteriorhodopsin as a model for these clinically important membrane proteins. This procedure includes (i) solubilization of the protein digest in acetic acid; and (ii) electrophoresis using an acetic acid-based buffer system augmented by acetonitrile and hexane sulfonic acid, in a Polybrenecoated fused silica capillary. The potential for detection sensitivity to be increased at least 100-fold by use of on-line solid-phase extraction on C18-silica is shown. This approach is potentially useful for peptide fingerprinting of sparse and extremely hydrophobic membrane receptors.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150181010
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  • 7
    Electronic Resource
    Electronic Resource
    Differential diagnosis of gammopathies by capillary electrophoresis and immunosubtraction: Analysis of serum samples problematic by agarose gel electrophoresis (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 2479-2484 
    Details
    ISSN: 0173-0835
    Keywords: Capillary electrophoresis ; Serum proteins ; Immunosubtraction ; Immunofixation electrophoresis ; Monoclonal protein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The capabilities of capillary electrophoresis (CE) for serum protein electrophoresis and immunotyping have been demonstrated. CE-based systems specifically designed for serum protein electrophoresis and immunotyping via immunosubtraction (IS) are now available and are being evaluated for efficiency, specificity and sensitivity by several groups. The use of CE for serum protein electrophoresis and immunotyping (IS) in the clinical laboratory compares well with agarose gel electrophoresis (AGE) and immunofixation (IF) for the detection and characterization of monoclonal proteins. In addition to routine use, this technology is useful for a subset of serum samples that are difficult to interpret with conventional technology. In this study, sera abnormalities difficult to detect/interpret by AGE-IF are subdivided into four categories: (i) patients with polyclonal increases in immunoglobulin, (ii) point of application artifacts, (iii) abnormalities in the beta region, and (iv) patients with free light chains. CE is superior to AGE for evaluating samples characterized by the above abnormalities. Sera containing monoclonal proteins within a polyclonal increase are easier to detect by CE as well as being easier to type by IS than by IF. Point-of-application artifacts, periodically observed with AGE, do not exist on CE since the point of detection is remote from the point of application. Enhanced resolution in the beta region allows for increased detection of monoclonal proteins migrating in this region. Some free light chains are undetected by CE as a result of no apparent abnormalities on the CE serum protein profile and, thus, still require IF for detection. CE detects more serum electrophoretic abnormalities than AGE in this clinically important group of patients with Bence Jones proteinemia.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150191421
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  • 8
    Electronic Resource
    Electronic Resource
    Charged chelate - capillary electrophoresis of endogenous corticosteroids (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 3045-3051 
    Details
    ISSN: 0173-0835
    Keywords: Borate ; Charged chelate ; Corticosteroids ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Separation of endogenous 17- or 18-hydroxylated corticosteroids (of the 21-hydroxylated 4-pregnen series) as charged chelates in capillary electrophoresis with borate as the ligand is demonstrated. Aldosterone, 18-hydroxycorticosterone, 18-hydroxy-11-deoxycorticosterone, cortisone, cortisol, and 11-deoxycortisol are separated and resolved by 400 mM borate buffer at pH 9.0. Separation characteristics of the corticosteroid charged chelates were examined by varying the separation buffer borate concentration, pH, ionic strength, and addition of organic modifiers. The borate ion [B(OH)4]- is identified as the critical buffer component. Corticosteroids chelate borate with proximal hydroxyls composed of either the 17- or 18-hydroxyl in combination with the 21-position hydroxyl. Corticosteroid/borate chelation as indicated by CE results is corroborated with 11B-nuclear magnetic resonance (11B-NMR) sprectra. Chelation is a readily reversible process, with the strength of the resultant chelate, as opposed to the charge-to-mass ratio, predominantly determining analyte mobility in charged chelate - capillary electrophoresis (CC-CE).
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150191642
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  • 9
    Electronic Resource
    Electronic Resource
    Capillary electrophoresis-based separation of transferrin sialoforms in patients with carbohydrate-deficient glycoprotein syndrome (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 1819-1826 
    Details
    ISSN: 0173-0835
    Keywords: Carbohydrate-deficient transferrin ; Glycosylation ; Sialic acid ; Physical gel ; Sieving matrix ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The heterogeneity associated with protein glycoforms has been a challenge to analytical chemists and the subject of structure-function studies for biochemists since their presence in biological systems had been confirmed some three decades ago. Initial investigations led to discoveries of synthetic and degradative pathways, and brief forays into functional determination of the “glyco” portion on the protein activity in glycoproteins. Only recently has it come to our understanding that variations from the “normal” glycosylation patterns might be indicative of pathological states. The presence of certain transferrin (Tf) glycoforms in human serum has been shown to correlate with certain clinical syndromes. Hence, the ability to separate and quantitatively measure the various forms of human Tf has become increasingly important. It this study, we demonstrate that a simple method utilizing a DB-17-coated capillary to slow endoosmotic flow and a sieving buffer containing hydroxyethyl cellulose allows for the resolution of sialoforms of transferrin. An analysis time of less than eight minutes allows for baseline resolution of the lower sialoforms of Tf, presenting a simple, rapid test for carbohydrate-deficient transferrin (CDT). We demonstrate the utility of this methodology for the facile diagnosis of carbohydrate-deficient glycoprotein syndrome, and postulate that it may allow for the detection of other carbohydrate-deficient protein-related disease states.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150181017
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  • 10
    Electronic Resource
    Electronic Resource
    Development of a nonisotopic capillary electrophoresis-based method for measuring glomerular filtration rate (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 1827-1835 
    Details
    ISSN: 0173-0835
    Keywords: Iothalamate ; Capillary electrophoresis ; Glomerular filtration rate ; Renal function ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The conditions for quantitative measurement of nonisotopic iothalamate meglumine (Conray) in urine and plasma by capillary zone electrophoresis (CE) have been developed. The impetus for developing this methodology was to replace the traditional [125I]iothalamate glomerular filtration rate (GFR) marker assay, a routine tool in the measurement of kidney function. This new approach for measuring kidney function is attractive since it avoids the cost of administration of radioisotopic compounds to patients, as well as the cost associated with purchase and disposal of isotopic compounds and contaminated samples. The concentration of iothalamate in urine and plasma determined by CE can be used directly to calculate GFR. The GFR in patients injected with [125I]iothalamate and nonisotopic iothalamate simultaneously showed an excellent correlation (0.998) with between-day coefficient of variation of 2.30% and a recovery of 102% and 98%, respectively, when added to urine and plasma. Interference from drugs and other urinary compounds is eliminated with this method. Collectively, this study has shown that CE is a cost-effective alternative to the current methodology for measuring GFR.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150181018
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