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  • 1.
    Bohlin, Maria E
    et al.
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Blomberg, Lars G.
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Heegaard, Niels H H
    Statens Serum Institut, Copenhagen.
    Effects of ionic strength, temperature and conformation on affinity interactions of β2-glycoprotein I monitored by capillary electrophoresis2011In: Electrophoresis, ISSN 0173-0835, E-ISSN 1522-2683, Vol. 32, p. 728-737Article in journal (Refereed)
    Abstract [en]

    We have used CE to evaluate the interaction between β2-glycoprotein I (β2gpI) and heparin. β2gpI is a human plasma protein involved in the blood coagulation cascade. It is of interest to functionally characterize the interactions of β2gpI because the exact function is not entirely known and because circulating autoantibodies against β2gpI are associated with an increased risk of thrombotic events.

     

    The effect of the ionic strength, temperature, and conformation of the protein on the interaction between β2gpI and heparin has been studied. The CE procedure for this study is simple, fast and automatic. β2gpI and heparin were allowed to interact during electrophoresis at different ionic strength buffers and at different capillary temperatures. To mimic perturbation of the conformation of β2gpI, different denaturing agents (SDS, ACN and urea) were added to the background electrolyte. While simple 1:1 binding isotherms were obtained at 22 °C the data strongly suggests that at physiological temperature the binding stoichiometry is not 1:1 and/or that cooperative interactions begin to play a role. We found that (i) the KD values differed by a factor of 60 at the ionic strengths studied (ii) β2gpI was resistant to denaturation with SDS and ACN, but was partially denatured by urea and (iii) the KD for the β2gpI-heparin interaction in the presence of urea was 10 times higher than the KD determined at the same conditions without urea added. Therefore, we conclude that the interaction between β2gpI and heparin is dependent on electrostatic interactions and on the conformation of β2gpI. 

  • 2.
    Bohlin, Maria E.
    et al.
    Karlstad University, Division for Chemistry.
    Blomberg, Lars G.
    Karlstad University, Division for Chemistry.
    Heegard, Niels H.H.
    Department of Autoimmunology, Statens Serum Institut, Copenhagen.
    Utilizing the pH hysteresis effect for versatile and simple electrophoretic analysis of protein in bare fused-silica capillaries2005In: Electrophoresis, ISSN 0173-0835, E-ISSN 1522-2683, Vol. 26, no 21, p. 4043-4049Article in journal (Refereed)
  • 3.
    Bohlin, Maria
    et al.
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Johannesson, Ida
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Carlsson, Gunilla
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Heegaard, Nils H H
    Department of Clinical Biochemistry and Immunology, Statens Serum Institut, Copenhagen, Denmark.
    Blomberg, Lars G.
    Karlstad University, Faculty of Technology and Science, Department of Chemistry and Biomedical Sciences.
    Estimation of the amount of β2-glycoprotein I adsorbed at the inner surface of fused silica capillaries after acidic, neutral and alkaline pretreatment2012In: Electrophoresis, ISSN 0173-0835, E-ISSN 1522-2683, Vol. 33, no 12, p. 1695-1702Article in journal (Refereed)
    Abstract [en]

    Sample adsorption to the inner surface of fused silica capillaries is a common problem in

    CE when analyzingmacromolecules and is harmful to the analysis. We previously utilized

    the pH hysteresis effect of fused silica to facilitate electrophoresis of the strongly adsorbing

    protein β2gpI in plain-fused silica capillaries at neutral pH. In the present paper, the

    effect of different pretreatments of the capillary on the adsorption of the β2-glycoprotein

    I has been investigated using electroosmosis markers, SDS mobilization, and imaging

    based on indirect immunofluorescence microscopy for direct visualization. The amount

    of β2gpI adsorbed on the surface was probed using all these independent techniques after

    electrophoresis at neutral pH on capillaries pretreated with HCl, background electrolyte

    (BGE), and NaOH. BGE pretreatment was included as a positive control. We found that

    80% or more of the starting material was adsorbed to the inner surface of the silica

    capillaries during electrophoresis after pretreatment with only BGE or with NaOH, but

    after acidic pretreatment the loss was consistently less than 20%. NaOH most efficiently

    removes adsorbed protein between runs. A theoretical calculation of the pH change of

    the BGE showed that electrolysis affects the pH more than the deprotonation of silanols

    during electrophoresis. We conclude that acidic pretreatment of fused silica capillaries

    diminishes adsorption of β2gpI by decreasing charge-dependent wall adsorption.

     

  • 4.
    Elhamili, Anisa
    et al.
    Uppsala University, Sweden.
    Samuelsson, Jörgen
    Uppsala universitet.
    Bergquist, Jonas
    Uppsala University, Sweden.
    Wetterhall, Magnus
    Uppsala University, Sweden.
    Optimizing the extraction, separation and quantification of tricyclic antidepressant drugs in human plasma with CE-ESI-TOF-MS using cationic-coated capillaries2011In: Electrophoresis, ISSN 0173-0835, E-ISSN 1522-2683, Vol. 32, no 6-7, p. 647-658Article in journal (Refereed)
    Abstract [en]

    In this study, the extraction and CE-ESI-TOF-MS analysis of tricyclic antidepressant (TCA) drugs imipramine, desipramine, clomipramine and norclomipramine in human plasma has been optimized. The CE capillaries were modified with omega-iodo-alkyl ammonium salt (M7C4I coating) to reduce analyte adsorption to the silica wall. The use of a strong cation exchange (SCX) solid-phase extraction (SPE) column specifically designed for the extraction of basic drug species from biofluids gave very clean extracts with high and reproducible recoveries. The extraction recoveries were ranging between 87 and 91% with % RSD values of 0.5-1.7% (n = 3). The obtained strong cation exchange-SPE extracts of the TCA in human plasma only contained the analytes of interest. The optimized CE separation conditions were obtained by adding ACN and acetic acid to the sample while using an aqueous BGE. The CE-ESI-TOF-MS analysis was performed within 6 min for all TCA analytes under the optimized condition with peak efficiencies up to 1.4 x 10(5) plates/m and an average % RSD of the migration times of the analytes of 0.3% (n = 5). The presented method can readily be used for the extraction and quantification of basic drug species in human biological fluids and in pharmaceutical formulations.

  • 5.
    Eriksson, Björn
    et al.
    Karlstad University, Faculty of Technology and Science.
    Dahl, Magnus
    Karlstad University, Faculty of Technology and Science.
    Andersson, Magnus
    Department of Analytical Chemistry, Pharmaceutical and Analytical Research & Development, AstraZeneca, Sweden.
    Blomberg, Lars
    Karlstad University, Faculty of Technology and Science.
    Changes in mobile phase ion distribution when combining pressurized flow and electric field2004In: Electrophoresis, ISSN 0173-0835, E-ISSN 1522-2683, Vol. 25, no 18-19, p. 3092-3097Article in journal (Refereed)
  • 6.
    Magnusson, Jeanette
    et al.
    Karlstad University, Faculty of Technology and Science.
    Wan, Hong
    Department of DMPK and Bioanalytical Chemistry, AstraZeneca R&D, Sweden.
    Blomberg, Lars G.
    Karlstad University, Faculty of Technology and Science.
    Illustration of a Simple and Versatile Scheme for Reversing Enantiomeric Elution Order and Facilitating Enantiomeric Impurity Determination in Capillary Electrophoresis2002In: Electrophoresis, ISSN 0173-0835, E-ISSN 1522-2683, Vol. 23, no 17, p. 3013-3019Article in journal (Refereed)
1 - 6 of 6
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