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  • 151.
    M.E., Schimpf and K.D. Caldwell
    Uppsala University, Centre for Surface Biotechnology.
    Electrical Field-Flow Fractionation for Colloid and Particle Analysis1995In: American Laboratory, p. 64-68Article in journal (Refereed)
  • 152.
    Neff, J. and Caldwell, K.D.
    Uppsala University, Centre for Surface Biotechnology.
    Surface Modification of Biomaterials.1999In: A. von Recum, (ed.), Handbook of Biomaterials, Taylor & Francis, Philadelphia , 1999, p. 201-226Chapter in book (Other scientific)
  • 153.
    Neff, J.A., Caldwell, K.D. and Tresco, P.A.
    Uppsala University, Centre for Surface Biotechnology.
    A Novel Method for Surface Modification to Direct Cell Behavior1998In: J. Biomed. Mat. Res., Vol. 40, p. 511-519Article in journal (Refereed)
  • 154.
    Nowotny N., Bascunana C.R., Ballagi-Pordany A., Gavier-Widen, D., Uhlen, M. and Belak, S.
    Uppsala University, Centre for Surface Biotechnology.
    Phylogenetic analysis of rabbit haemorrhagic disease and European brown hare syndrome viruses by comparison of sequences from the capsid protein gene1997In: Arch Virol, Vol. 142, no 4, p. 657-673Article in journal (Refereed)
  • 155.
    Oscarsson, S.
    Uppsala University, Centre for Surface Biotechnology.
    Surface Functionalisation, Orientation, Confirmation and Positioning of Macromolecules at the Nanometer Scale2002In: International Journal of Nonlinear Sciences and Numerical Simulations, p. 747-749Article in journal (Refereed)
  • 156.
    Oscarsson, S.
    et al.
    Uppsala University, Centre for Surface Biotechnology.
    Batista-Viera, F.
    Thiophilic Interaction Chromatography2002In: Biochromatography, Chapter 11, London and New York: Taylor and Francis , 2002, p. 295-306Chapter in book (Other scientific)
  • 157.
    Oscarsson.S,
    Uppsala University, Centre for Surface Biotechnology.
    Methods of Protheic Analysis by Chromatography and AFM1995In: 2: nd Meeting and Seminar on: Ceramics,Cells and Tissues, 1995, (Ed. A.Ravaglioli, and Krajewski,A.), Gruppo editoriale Faenza editrice., 1995, p. 146-153Conference paper (Other scientific)
  • 158.
    Ovsejevi, K., Brena, B., Batista-Viera, F. and Carlsson, J.
    Uppsala University, Centre for Surface Biotechnology.
    Immobilization of b-galactosidase on thiolsulfonate-agarose1995In: Enzyme and Microb. Technol., Vol. 17, p. 151-156Article in journal (Refereed)
  • 159.
    Pathmasiri, Wimal
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Division of Pharmacognosy.
    el-Seedi, Hesham R
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Division of Pharmacognosy.
    Han, Xiao
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology, Centre for Surface Biotechnology.
    Janson, Jan-Christer
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology, Centre for Surface Biotechnology.
    Huss, Ulrika
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Division of Pharmacognosy.
    Bohlin, Lars
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Division of Pharmacognosy.
    Aryl ketones from Acronychia pedunculata with cyclooxygenase-2 inhibitory effects2005In: Chemistry & biodiversity, ISSN 1612-1872, Vol. 2, no 4, p. 463-469Article in journal (Refereed)
    Abstract [en]

    1-[2,4-Dihydroxy-6-methoxy-3,5-bis(3-methylbut-2-en-1-yl)phenyl]ethanone (1), and a new aryl ketone, named acrovestenol (2), were isolated as cyclooxygenase-2 (COX-2) inhibitory principles from a CH2Cl2 extract of the bark of Acronychia pedunculata by a bioassay-guided fractionation procedure. Compound 2 inhibited COX-2 with an IC50 value of 142.0+/-2.15 microM, compared to the COX-2 inhibitory reference compound NS-398 with an IC50 value of 11.3+/-1.12 microM. Compound 1 inhibited COX-2-catalyzed PG biosynthesis with 68% at a concentration of 500 microM. The structures were determined by UV, IR, and 1D- and 2D-NMR, including TOCSY, HSQC-DEPT, and HMBC, and MS investigations.

  • 160.
    Pavlovic, E.
    et al.
    Uppsala University, Centre for Surface Biotechnology.
    Quist, A. P.
    Gelius, U.
    Oscarsson, S.
    Development of a flow method for surface functionalization at room temperature and ambient pressure2002In: J. Colloid Interface Science, Vol. 254, p. 200-203Article in journal (Refereed)
  • 161.
    Persson, L.
    et al.
    Uppsala University, Centre for Surface Biotechnology.
    Whitlow, H. J.
    El Bouanani, M.
    Hult, M.
    Andersson, M.
    Bubb, I. F.
    Johnston, P. N.
    Walker, S. R.
    Cohen, D. D.
    Dytlewski, N.
    Zaring, C.
    Östling, M.
    Separation of mass overlapped recoil spectometry data using Ryan and Jamieson's dynamic analysis method2001In: Nuclear Instr. and Meth. B, Vol. 179, p. 403-411Article in journal (Refereed)
  • 162. Pettersson, Torbjörn
    et al.
    Nordgren, Niklas
    Rutland, Mark W.
    Feiler, Adam
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Comparison of different methods to calibrate torsional spring constant and photodetector for atomic force microscopy friction measurements in air and liquid2007In: Review of Scientific Instruments, ISSN 0034-6748, E-ISSN 1089-7623, Vol. 78, no 9, p. 093702-093702-8Article in journal (Refereed)
    Abstract [en]

    A number of atomic force microscopy cantilevers have been exhaustively calibrated by a number of techniques to obtain both normal and frictional force constants to evaluate the relative accuracy of the different methods. These were of either direct or indirect character—the latter relies on cantilever resonant frequencies. The so-called Sader [Rev. Sci. Instrum. 70, 3967 (1999)] and Cleveland [Rev. Sci. Instrum. 64, 403 (1993)] techniques are compared for the normal force constant calibration and while agreement was good, a systematic difference was observed. For the torsional force constants, all the techniques displayed a certain scatter but the agreement was highly encouraging. By far the simplest technique is that of Sader, and it is suggested in view of this validation that this method should be generally adopted. The issue of the photodetector calibration is also addressed since this is necessary to obtain the cantilever twist from which the torsional force is calculated. Here a technique of obtaining the torsional photodetector sensitivity by combining the direct and indirect methods is proposed. Direct calibration measurements were conducted in liquid as well as air, and a conversion factor was obtained showing that quantitative friction measurements in liquid are equally feasible provided the correct calibration is performed.

  • 163.
    Porath, Jerker
    Uppsala University, Centre for Surface Biotechnology.
    Strategy for Differential Protein Affinity Chromatrography2001In: IJBC, Vol. 6, no 1, p. 51-78Article in journal (Refereed)
  • 164.
    Puerta, Angel
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Analytical Chemistry.
    Axén, Jakob
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Analytical Chemistry.
    Söderberg, Lennart
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Bergquist, Jonas
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Analytical Chemistry.
    Novel adsorptive polyamine coating for enhanced capillary electrophoresis of basic proteins and peptides2006In: Journal of chromatography. B, ISSN 1570-0232, E-ISSN 1873-376X, Vol. 838, no 2, p. 113-121Article in journal (Refereed)
    Abstract [en]

    In capillary electrophoresis (CE), the anionic and hydrophobic nature of the fused-silica capillary surface has long been known to present a problem in protein and peptide analysis. The use of capillary surface coating is one of the approaches to avoid the analyte-wall interactions. In this study, a new polymer, poly-LA 313, has been synthesized, physico-chemical characterized, and applied as polyamine coating for CE separations. The coating process is highly reproducible and provides fast separations of peptides and proteins in a few minutes and with high efficiency. The physically adsorbed polymer gives rise to a durable coating in the range of pH 2-10, in the presence of organic modifiers (acetonitrile and methanol) and with complex biological samples. The efficiency of the new cationic polymer was also tested performing protein and peptide separations with capillary electrophoresis-electrospray ionization-mass spectrometry (CE-ESI-MS).

  • 165.
    Pålsgard, Eva
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology, Centre for Surface Biotechnology.
    Dijksterhuis, G
    The sensory perception of flavor release as a function of texture and time: A time intensity study using flavored gels2000In: Journal of sensory studies, ISSN 0887-8250, E-ISSN 1745-459X, Vol. 15, no 3, p. 347-359Article in journal (Refereed)
    Abstract [en]

    The focus in this study was to study time intensity (TI) methodology and procedures of getting thesensory panel acquainted with this technique. By means of a descriptive profiling exercise effects ofaltering the structure of a beta-lactoglobulin gel, laced with banana aroma on the perception of bananaflavor were obtained and a suitable attribute for TI was selected. Samples made up by protein, without any fat are not ideal for a TI study of flavor release because of the fast release of aroma. However, although the concentration of banana aroma was identical in the four groups of gels the intensity was perceived as different. This was reflected in the descriptive profiling as well as in the dynamic study.The TI study showed that it is important to minimize distractive, noncrucial information during theexercise. The assessors had different abilities to connect with the dynamic data acquisition procedure and training made the assessments more congruent. The results also indicate a relationship betweenthe appearance of the TI-curve and the score of the total banana aftertaste.

  • 166.
    Pålsgård, Eva
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology, Centre for Surface Biotechnology.
    Lindh, U
    Roomans, G M
    Grime, G W
    Tetrahydrofuran Freeze-Substituted Pancreas Analysed by Nuclear Microscopy and X-ray Microanalysis1996In: Journal of trace and microprobe techniques (Print), ISSN 0733-4680, E-ISSN 1532-2270, Vol. 14, no 3, p. 615-631Article in journal (Refereed)
    Abstract [en]

    A new freeze-substitution method using tetrahydrofuran (THF) as organic solvent was tested in the preparation of pancreas for determination of elemental content and distribution. Particle induced X-rayemission (PIXE) allowed analysis at the cellular level and X-ray microanalysis (EPMA) at the subcellular level. Using PIXE allowed detection of Zn, Ca and Fe, not detectable in the EPMA spectra. The ratios of Cl and K to P and to S obtained from analysis using both PIXE and EPMA agreed well. A good preservation of the in vivo ionic content was manifested in high K to Na and K to Cl ratios.

  • 167.
    Pålsgård, Eva
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology, Centre for Surface Biotechnology.
    Ugarte, M
    Rajta, I
    Grime, GW
    The role of zinc in the dark-adapted retina studied directly using microPIXE2001In: Nuclear Instruments and Methods in Physics Research Section B: Beam Interactions with Materials and Atoms, ISSN 0168-583X, E-ISSN 1872-9584, Vol. 181, p. 489-492Article in journal (Refereed)
    Abstract [en]

    Zinc deficiency is known to cause night blindness, which can be reverted by the administration of zinc.The exact function of zinc is not understood but it is likely that zinc plays a unique role in thephototransduction process and/or photoreceptor/retinal pigment interaction. The localisation of free (histochemically reactive) zinc within the photoreceptors changes with light stimulation [Exp. Eye Res. (1999) 459]. In the dark-adapted retina chelatable zinc can be visualised primarily in the perikarya, whereas after photostimulation free zinc is mainly associated with the inner segments. This variation might be due to (1) a translocation of zinc from the perikarya to the inner segments, (2) a change in thestate of zinc (from a free to a bound form, histochemically and non-histochemically reactive, respectively), or (3) zinc influx and/or efflux across the plasma membrane. MicroPIXE was used to analyse the total (free and bound) zinc distribution in each retinal layer and a difference was found between light- and dark-adapted retinas (preliminary data). Following light stimulation the most pronounced difference in the zinc concentration was found in the inner segments of the photoreceptors and the layer containing the photoreceptors perikarya (outer nuclear layer).

  • 168.
    Q. Zhao, I. Gottschalk, J. Carlsson, L.-E. Arvidsson, S. Oscarsson, A. Medin, B. Ersson and J.-C. Janson
    Uppsala University, Centre for Surface Biotechnology.
    Preparation and Purification of an End to End Coupled mEGF-Dextran Conjugate1997In: Bioconjugate Chemistry, Vol. 8, no 6, p. 927-934Article in journal (Refereed)
  • 169.
    Q. Zhao, V. Tolmachev, J. Carlsson, H. Lundqvist, J. Sundin, J.-C. Janson and A. Sundin
    Uppsala University, Centre for Surface Biotechnology.
    Influence of conjugation to dextran on the pharmacokinetics of mouse epidermal growth factor (EGF)1998In: Tumor Biology, Vol. 19, no 2, p. 45-Article in journal (Refereed)
  • 170.
    R. Parsons, V. Yue, X. Tong, P. Cardot, A. Bernard, J.P. Andreux, and K.D. Caldwell
    Uppsala University, Centre for Surface Biotechnology.
    A Comparative Study of Human Red Blood Cell Analysis with Three Different Field-Flow Fractionation Systems1996In: J. Chromatogr. B, Vol. 686, p. 177-187Article in journal (Refereed)
  • 171. Ralston, John
    et al.
    Larson, Ian
    Rutland, Mark W.
    Feiler, Adam A.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Kleijn, Mieke
    Atomic force microscopy and direct surface force measurements2005In: Pure and Applied Chemistry, ISSN 0033-4545, Vol. 77, no 12, p. 2149–2170-Article in journal (Refereed)
    Abstract [en]

    IUPAC Physical and Biophysical Chemistry Division

    The atomic force microscope (AFM) is designed to provide high-resolution (in the ideal case, atomic) topographical analysis, applicable to both conducting and nonconducting surfaces. The basic imaging principle is very simple: a sample attached to a piezoelectric positioner is rastered beneath a sharp tip attached to a sensitive cantilever spring. Undulations in the surface lead to deflection of the spring, which is monitored optically. Usually, a feedback loop is employed, which holds the spring deflection constant, and the corresponding movement of the piezoelectric positioner thus generates the image. From this it can be seen that the scanning AFM has all the attributes necessary for the determination of surface and adhesion forces; a sensitive spring to determine the force, a piezoelectric crystal to alter the separation of the tip and surface, which if sufficiently well-calibrated also allows the relative separation of the tip and surface to be calculated. One can routinely quantify both the net surface force (and its separation dependence) as the probe approaches the sample, and any adhesion (pull-off) force on retraction. Interactions in relevant or practical systems may be studied, and, in such cases, a distinct advantage of the AFM technique is that a particle of interest can be attached to the end of the cantilever and the interaction with a sample of choice can be studied, a method often referred to as colloid probe microscopy. The AFM, or, more correctly, the scanning probe microscope, can thus be used to measure surface and frictional forces, the two foci of this article. There have been a wealth of force and friction measurements performed between an AFM tip and a surface, and many of the calibration and analysis issues are identical to those necessary for colloid probe work. We emphasize that this article confines itself primarily to elements of colloid probe measurement using the AFM.

  • 172.
    Rosengren, Å.
    et al.
    Uppsala University, Centre for Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Pavlovic, E.
    Uppsala University, Centre for Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Oscarsson, S.
    Uppsala University, Centre for Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Krajewski, A.
    Ravaglioli, A.
    Piancastelli, A.
    Plasma protein adsorption pattern on characterized ceramic biomaterials2002In: Biomaterials, Vol. 23, p. 1237-1247Article in journal (Refereed)
  • 173.
    Rosengren, Å.
    et al.
    Uppsala University, Centre for Surface Biotechnology.
    Pavlovic, E.
    Oscarsson, S.
    Ravaglioli, A.
    Krajewski, A.
    Piancastelli, A.
    In vitro studies of the interface between human plasma proteins and bone graft substitutes2001In: Proceedings 7th Seminar and Meetings; Biomimetic Engineering June 13-15, 2001, Faenza, Italy, Gruppo editoriale faenza editrice s.p.a. , 2001, p. 169-171Conference paper (Refereed)
  • 174.
    Rosengren, Åsa
    et al.
    Uppsala University, Centre for Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Oscarsson, Sven
    Uppsala University, Centre for Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Protein adsorption onto biomaterials after exposure to human serum1997In: 4: th Meeting and Seminars on Ceramic - Polymer Composites, May 22 - 24, 1997. Faenza, Italy. (Ed. Ravaglioli, A. and Krajewski, A.).Gruppo editoriale faenza editrice s.p.a., 1997, p. 207-211Conference paper (Other scientific)
  • 175.
    Rosengren, Åsa
    et al.
    Uppsala University, Centre for Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Oscarsson, Sven
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Protein adsorption onto biomaterials after exposure to human serum1998In: 5: th Meeting and Seminars on Ceramics, Cells and Tissues. Oct. 1-3, 1998, Faenza, Italy (Ed. Ravaglioli, A. and Krajewski, A.).Gruppo editoriale faenza editrice s.p.a., 1998Conference paper (Other scientific)
  • 176.
    Rundström, Gerd
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Surface Biotechnology.
    Jonsson, Ann
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology, Centre for Surface Biotechnology.
    Mårtensson, Ola
    Mendel-Hartvig, Ib
    Venge, Per
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences, Clinical Chemistry.
    Lateral Flow Immunoassay Using Europium (III) Chelate Microparticles and Time-Resolved Fluorescence for Eosinophils and Neutrophils in Whole Blood2007In: Clinical Chemistry, ISSN 0009-9147, E-ISSN 1530-8561, Vol. 53, no 2, p. 342-348Article in journal (Refereed)
    Abstract [en]

    Background: A simple point-of-care method for measuring leukocyte counts in a doctor’s office or emergency room could be of great importance. We developed a protocol for measuring cell count by disrupting the cell membrane and analyzing specific proteins within the cells and used it to analyze proteins from eosinophils and neutrophils.

    Methods: Lateral immunochromatographic (ICR) assays have been developed for eosinophil protein X (EPX) and human neutrophil lipocalin (HNL) as measures of the concentration of eosinophils and neutrophils. The correlation between the lateral ICR assays and cell counting of eosinophils and neutrophils was performed manually and with an automated cell counter. RIA assays measuring the same analytes were also compared with the results from cell counting and lateral ICR assays.

    Results: The optimized assays showed analytical detection limits below the clinical ranges of 3.36 µg/L and 2.05 µg/L for EPX and HNL, respectively. The recovery was 114.8%–122.8% for EPX and 94.5%–96.9% for HNL. The imprecision was 3%–17% CV for EPX over the whole range and 5%–16% CV for HNL. The correlation coefficients between manually counted cells and lateral ICR assays were 0.9 and 0.83 for EPX and HNL, respectively.

    Conclusion: The numbers of eosinophils and neutrophils in small amounts of blood can be estimated in the point-of-care setting by means of fast lateral ICR assays of EPX and HNL.

  • 177.
    Samuelsson, Jörgen
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Development of Methods for Phase System Characterization in Liquid Chromatography2008Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

    The aim of this thesis is first and foremost to improve the fundamental knowledge of nonlinear and preparative separation theory by focusing on some of the remaining “white spots” on the theoretical chromatographic map. Secondly, the acquired knowledge is used to develop, validate and execute new methods for phase characterization in liquid chromatography. The methodology used in this thesis is a combination of experiments, fundamental nonlinear theory and systematic computer simulations.

    A fundamental knowledge of the molecular interactions between the compounds to be separated and the separation media requires the determination of adsorption isotherms over a broad concentration range to give a complete picture of all interactions in the separation system - weak as well as strong. In addition, such adsorption data is essential for optimization in preparative chromatography.

    For the first time, it has been experimentally shown that the injected molecules are not present in the detected peak when a small excess of molecules are injected into a chromatographic system equilibrated with a constant stream of identical molecules. Several experimental procedures for this method were developed such as (i) the optimal injection strategy and (ii) different labeling methods for visualizing the injected molecules. Remarkable phenomena in the single-component case, such as invisible peak deformation and deformed (invisible) frontal chromatograms, are reported, investigated, and explained. This phenomenon has asides from its future practical implementation, also a large didactic value.

    The accuracy of the ECP method is experimentally improved, and used to characterize the separation of protolytic compounds at different pH on modern commercially available silica and hybrid silica column packing materials. That investigation enables us to answer why basic compounds give a much more compact preparative peak profile at pH 11 than they yields at lower pH.

    List of papers
    1. Experimental Proof of a Chromatographic Paradox: Are the injected molecules in the peak?
    Open this publication in new window or tab >>Experimental Proof of a Chromatographic Paradox: Are the injected molecules in the peak?
    2004 (English)In: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 76, p. 953-958Article in journal (Refereed) Published
    National Category
    Analytical Chemistry Computational Mathematics
    Identifiers
    urn:nbn:se:uu:diva-96953 (URN)10.1021/ac030268j (DOI)
    Available from: 2008-04-04 Created: 2008-04-04 Last updated: 2018-01-23Bibliographically approved
    2. Discovery of invisible extra fronts in single-component frontal analysis in liquid chromatography
    Open this publication in new window or tab >>Discovery of invisible extra fronts in single-component frontal analysis in liquid chromatography
    2006 (English)In: Journal of Chromatography A, ISSN 0021-9673, E-ISSN 1873-3778, Vol. 1114, no 1, p. 53-61Article in journal (Refereed) Published
    Abstract [en]

    Frontal analysis (FA) is often used in the “staircase mode”, in which the solute concentration in the eluent increases stepwise. We demonstrate here in the single-component case, that all eluted breakthrough curves (fronts) for the second and subsequent steps consist solely of displaced plateau molecules. The newly introduced molecules (i.e., the introduced mass) instead elute later, in a breakthrough front hidden from detection, i.e., the mass front. These effects were studied using experimentally verified numerical calculations, the mass fronts being visualized using an enantiomer pair in an achiral separation system. Notably, the mass front displays no self-sharpening effects, even under strongly nonlinear conditions. Instead, the front is sigmoidal in shape.

    National Category
    Chemical Sciences
    Identifiers
    urn:nbn:se:uu:diva-96954 (URN)10.1016/j.chroma.2006.02.027 (DOI)
    Available from: 2008-04-04 Created: 2008-04-04 Last updated: 2018-01-23Bibliographically approved
    3. Invisible Analyte Peak Deformations in Single-Component Liquid Chromatography
    Open this publication in new window or tab >>Invisible Analyte Peak Deformations in Single-Component Liquid Chromatography
    2006 (English)In: Analytical Chemistry, Vol. 78, no 8, p. 2765-2771Article in journal (Refereed) Published
    Identifiers
    urn:nbn:se:uu:diva-96955 (URN)
    Available from: 2008-04-04 Created: 2008-04-04 Last updated: 2009-03-20Bibliographically approved
    4. Development of the Tracer-Pulse method for adsorption studies of analyte mixures in liquid chromatography utilizing mass spectrometric detection
    Open this publication in new window or tab >>Development of the Tracer-Pulse method for adsorption studies of analyte mixures in liquid chromatography utilizing mass spectrometric detection
    Show others...
    2008 (English)In: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 80, no 6, p. 2105-2112Article in journal (Refereed) Published
    Abstract [en]

    The tracer-pulse method provides the real adsorption data points directly from simple, straightforward calculations and is therefore a superior method for multicomponent adsorption isotherm determination in HPLC. Only one important problem has restricted its use so far: the tracer peaks are invisible using any conventional detection principle. We present a solution to this problem with an approach with a firm base in analytical chemistry, utilizing stable isotopes and mass spectrometric detection. The new approach was used for the determination of binary adsorption isotherms, and a systematic investigation was made of its main sources of error. With this modification, the tracer method can be a prime choice for future characterizations of multicomponent separation systems and of competitive drug binding studies.

    National Category
    Chemical Sciences
    Identifiers
    urn:nbn:se:uu:diva-96956 (URN)10.1021/ac702399a (DOI)000254017000035 ()18290673 (PubMedID)
    Available from: 2008-04-04 Created: 2008-04-04 Last updated: 2017-12-14Bibliographically approved
    5. Development and Validation of a newly modified injection method for more accurate adsorption isotherm data using elution by characteristic points
    Open this publication in new window or tab >>Development and Validation of a newly modified injection method for more accurate adsorption isotherm data using elution by characteristic points
    (English)Manuscript (Other (popular science, discussion, etc.))
    Identifiers
    urn:nbn:se:uu:diva-96957 (URN)
    Available from: 2008-04-04 Created: 2008-04-04 Last updated: 2010-01-14Bibliographically approved
    6. Thermodynamic characterization of separations on alkaline-stable silica-based C18 columns: Why basic solutes may have better capacity and peak performance at higher pH
    Open this publication in new window or tab >>Thermodynamic characterization of separations on alkaline-stable silica-based C18 columns: Why basic solutes may have better capacity and peak performance at higher pH
    2007 (English)In: Journal of Chromatography A, ISSN 0021-9673, E-ISSN 1873-3778, Vol. 1163, no 1-2, p. 177-189Article in journal (Refereed) Published
    Abstract [en]

    A systematic study was made to explain the large improvements in separation performance and capacity of basic compounds at alkaline conditions. The adsorption of three probe components was investigated on four alkaline-stable silica-based C18 columns at three different pH-levels: 3, 7 and 11. The probes were 3-phenyl-1-propanol (neutral), 2-phenylbutyric acid (acidic) and metoprolol (basic). Adsorption isotherms were acquired over a broad concentration range, in order to detect both high and low energy sites. Before the choice of the proper adsorption isotherm model, the adsorption energy distribution (AED) was calculated yielding the number of different kinds of interaction sites between the solute and the stationary phase. The neutral probe was entirely unaffected by pH and its AED was unimodal (one site) indicating homogenous adsorption. For the acidic probe the interactions were unimodal at pH 3 where the probe is uncharged and at least bimodal (two sites) at pH 7 and 11 where the probe is charged. For the basic probe, the interactions were heterogeneous at both pH 3 and 11. The equilibrium constants of the high and low energy sites were different by a factor of 55–100 at pH 3 and only 6–7 at pH 11. The difference in saturation capacities between the two sites was much smaller at pH 11 where 20% of the total capacity is from the high energy site, as compared to pH 3 where the high energy site was only 2–5% of the total capacity. This explains why peaks of amines (basic solutes) tail at low pH while their peaks are symmetrical at alkaline pH. The Langmuir model fit the unimodal data and the bi-Langmuir model fit the bimodal AED data. The calculated band profiles based on these parameters agreed excellently with the experimental data. The electrostatic-modified Langmuir, on the other hand, did not describe this adsorption process well.

    Keywords
    Adsorption energy distribution, Adsorption isotherm, Alkaline conditions, Column characterization, Frontal analysis of characteristic points, Chromatography, FACP
    National Category
    Chemical Sciences
    Identifiers
    urn:nbn:se:uu:diva-96958 (URN)10.1016/j.chroma.2007.06.026 (DOI)000249310800018 ()17612549 (PubMedID)
    Available from: 2008-04-04 Created: 2008-04-04 Last updated: 2018-01-23Bibliographically approved
  • 178.
    Samuelsson, Jörgen
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Arnell, Robert
    Diesen, Jarle
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry.
    Tibbelin, Julius
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry.
    Paptchikhine, Alexander
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Fornstedt, Torgny
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Sjöberg, Per J. R.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Analytical Chemistry.
    Development of the Tracer-Pulse method for adsorption studies of analyte mixures in liquid chromatography utilizing mass spectrometric detection2008In: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 80, no 6, p. 2105-2112Article in journal (Refereed)
    Abstract [en]

    The tracer-pulse method provides the real adsorption data points directly from simple, straightforward calculations and is therefore a superior method for multicomponent adsorption isotherm determination in HPLC. Only one important problem has restricted its use so far: the tracer peaks are invisible using any conventional detection principle. We present a solution to this problem with an approach with a firm base in analytical chemistry, utilizing stable isotopes and mass spectrometric detection. The new approach was used for the determination of binary adsorption isotherms, and a systematic investigation was made of its main sources of error. With this modification, the tracer method can be a prime choice for future characterizations of multicomponent separation systems and of competitive drug binding studies.

  • 179.
    Samuelsson, Jörgen
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Arnell, Robert
    Fornstedt, Torgny
    Invisible Analyte Peak Deformations in Single-Component Liquid Chromatography2006In: Analytical Chemistry, Vol. 78, no 8, p. 2765-2771Article in journal (Refereed)
  • 180.
    Samuelsson, Jörgen
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Surface Biotechnology. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Arnell, Robert
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Surface Biotechnology. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Fornstedt, Torgny
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Surface Biotechnology. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Invisible Analyte Peak Deformations in Single-Component Liquid Chromatography2006In: Analytical Chemistry, Vol. 78, no 8, p. 2765-2771Article in journal (Refereed)
    Abstract [en]

    It is well known that if a small excess of solute is injected into a chromatographic system equilibrated with an eluent containing the same solute, a single so-called perturbation peak will appear in the chromatogram. It was recently shown (Samuelsson, J.; Forssén, P.; Stefansson, M.; Fornstedt, T. Anal. Chem. 2004, 76, 953-958) that this peak consists of displaced plateau molecules; the injected molecules (mass peak) elute later, together with a deficiency of plateau molecules and are therefore not detected. In this article, we investigated what happens if a large rather than a small excess of solute molecules is injected. To study this systematically, the experimental method involved an enantiomer pair in an achiral separation system. It was found that the invisible mass peak was extremely deformed and that its shape depended on the amount of excess injected, the eluent concentration, and the column length. Depending on these operational conditions, the mass peak changed from a classical Langmuirian (tailing) to an anti-Langmuirian (leading) shape, with deformed shapes observable in the transition. The visible, overloaded perturbation peak was always Langmuirian, regardless of the mass peak shape.

  • 181.
    Samuelsson, Jörgen
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Fornstedt, Torgny
    Development and Validation of a newly modified injection method for more accurate adsorption isotherm data using elution by characteristic pointsManuscript (Other (popular science, discussion, etc.))
  • 182.
    Samuelsson, Jörgen
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Surface Biotechnology.
    Fornstedt, Torgny
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Surface Biotechnology. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Discovery of invisible extra fronts in single-component frontal analysis in liquid chromatography2006In: Journal of Chromatography A, ISSN 0021-9673, E-ISSN 1873-3778, Vol. 1114, no 1, p. 53-61Article in journal (Refereed)
    Abstract [en]

    Frontal analysis (FA) is often used in the “staircase mode”, in which the solute concentration in the eluent increases stepwise. We demonstrate here in the single-component case, that all eluted breakthrough curves (fronts) for the second and subsequent steps consist solely of displaced plateau molecules. The newly introduced molecules (i.e., the introduced mass) instead elute later, in a breakthrough front hidden from detection, i.e., the mass front. These effects were studied using experimentally verified numerical calculations, the mass fronts being visualized using an enantiomer pair in an achiral separation system. Notably, the mass front displays no self-sharpening effects, even under strongly nonlinear conditions. Instead, the front is sigmoidal in shape.

  • 183.
    Samuelsson, Jörgen
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Surface Biotechnology. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Forssén, Patrik
    Uppsala University, Disciplinary Domain of Science and Technology, Mathematics and Computer Science, Department of Information Technology, Division of Scientific Computing.
    Stefansson, Morgan
    Fornstedt, Torgny
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Surface Biotechnology. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Experimental Proof of a Chromatographic Paradox: Are the injected molecules in the peak?2004In: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 76, p. 953-958Article in journal (Refereed)
  • 184.
    Samuelsson, Jörgen
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Franz, André
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Stanley, Brett
    Fornstedt, Torgny
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Thermodynamic characterization of separations on alkaline-stable silica-based C18 columns: Why basic solutes may have better capacity and peak performance at higher pH2007In: Journal of Chromatography A, ISSN 0021-9673, E-ISSN 1873-3778, Vol. 1163, no 1-2, p. 177-189Article in journal (Refereed)
    Abstract [en]

    A systematic study was made to explain the large improvements in separation performance and capacity of basic compounds at alkaline conditions. The adsorption of three probe components was investigated on four alkaline-stable silica-based C18 columns at three different pH-levels: 3, 7 and 11. The probes were 3-phenyl-1-propanol (neutral), 2-phenylbutyric acid (acidic) and metoprolol (basic). Adsorption isotherms were acquired over a broad concentration range, in order to detect both high and low energy sites. Before the choice of the proper adsorption isotherm model, the adsorption energy distribution (AED) was calculated yielding the number of different kinds of interaction sites between the solute and the stationary phase. The neutral probe was entirely unaffected by pH and its AED was unimodal (one site) indicating homogenous adsorption. For the acidic probe the interactions were unimodal at pH 3 where the probe is uncharged and at least bimodal (two sites) at pH 7 and 11 where the probe is charged. For the basic probe, the interactions were heterogeneous at both pH 3 and 11. The equilibrium constants of the high and low energy sites were different by a factor of 55–100 at pH 3 and only 6–7 at pH 11. The difference in saturation capacities between the two sites was much smaller at pH 11 where 20% of the total capacity is from the high energy site, as compared to pH 3 where the high energy site was only 2–5% of the total capacity. This explains why peaks of amines (basic solutes) tail at low pH while their peaks are symmetrical at alkaline pH. The Langmuir model fit the unimodal data and the bi-Langmuir model fit the bimodal AED data. The calculated band profiles based on these parameters agreed excellently with the experimental data. The electrostatic-modified Langmuir, on the other hand, did not describe this adsorption process well.

  • 185.
    Samuelsson, Jörgen
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Sajonz, Peter
    Fornstedt, Torgny
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Impact of an error in the column hold-up time for correct adsorption isotherm determination in chromatography: I. Even a small error can lead to a misunderstanding of the retention mechanism2008In: Journal of Chromatography A, ISSN 0021-9673, E-ISSN 1873-3778, Vol. 1189, p. 19-31Article in journal (Refereed)
    Abstract [en]

    The impact of a realistic error in the column hold-up time on the determination of the adsorption isotherm model was systematically investigated. Frontal analysis and the inverse method were used for the accurate determination of the adsorption isotherm. The true retention times of the breakthrough curves were used with a known hold-up time as reference. The adsorption isotherms were calculated using the same procedure that is used for real experimental adsorption isotherms, where the true hold-up time is unknown. The raw data were analyzed with calculations of adsorption energy distributions (AEDs), Scatchard plots, fitting to different rival adsorption models and finally their ability to predict true profiles. The results show that for a true Langmuir and bi-Langmuir model with an underestimated hold-up time the error may lead to a more heterogeneous model and for overestimated cases false adsorption processes like multi-layer adsorption or solute–solute interaction are assumed. The Scatchard plots for data obtained using a Langmuir adsorption isotherm are nonlinear and the AEDs show clear deviations from Langmuir behavior already at small deviations from the true hold-up time at a moderate surface coverage. The inverse method confirms the result that was obtained from the frontal analysis procedure.

  • 186.
    Samuelsson, Jörgen
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Zang, Jia
    Murunga, Anne
    Fornstedt, Torgny
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Sajonz, Peter
    Impact of an error in the column hold-up time for correct adsorption isotherm determination in chromatography: II. Can a wrong column porosity lead to a correct prediction of overloaded elution profiles?2008In: Journal of Chromatography A, ISSN 0021-9673, E-ISSN 1873-3778, Vol. 1194, no 2, p. 205-212Article in journal (Refereed)
    Abstract [en]

    The adsorption isotherm was determined for phenol in methanol/water on a C-8 stationary phase using frontal analysis in staircase mode, assuming different total column porosities, from 1 to 87%. Each set of adsorption isotherm data, with a certain column porosity, was fitted to various adsorption models and the generated parameters were used to calculate overloaded elution band profiles that were compared with experiments. It was found that the bi-Langmuir model had an optimum fit for a porosity that corresponds well with the value found experimentally. The adsorption energy distribution (AED) calculations and error analysis confirmed a bimodal energy distribution. It was also found that band profiles can be accurately predicted with a quite arbitrary chosen porosity, under prerequisite that a wrong but flexible adsorption model is chosen instead of the correct one. The latter result is very useful for quick optimizations of preparative separations where the exact value of the column porosity is not available.

  • 187.
    Sandberg, T
    et al.
    Uppsala University, Centre for Surface Biotechnology.
    Nestor, M
    Pahlson, C
    Shi, L
    Caldwell, KD
    Mucin as surface protectant against bacterial adhesion.2000In: ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, Vol. 220, p. 35-COLL -Other (Other scientific)
  • 188.
    Sandberg, Tomas
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Carlsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Karlsson Ott, Marjam
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Interactions between human neutrophils and mucin-coated surfaces2009In: Journal of materials science. Materials in medicine, ISSN 0957-4530, E-ISSN 1573-4838, Vol. 20, no 2, p. 621-631Article in journal (Refereed)
    Abstract [en]

    Recently, we showed microscopically that bovine (BSM), porcine (PGM) and human (MG1) mucin coatings could suppress the adhesion of neutrophils to a polyethylene terephthalate-based model biomaterial (Thermanox). Here, using the release of reactive oxygen species (ROS) as a marker of material-induced neutrophil activation, the strong surface-passivating effects of these mucin coatings were corroborated. Under optimal adsorption conditions, all mucin species performed equally well, thus indicating a high degree of functional homology between the mucins. Cell adhesion and morphology correlated well with the release of ROS. Quartz crystal microbalance (QCM-D) analysis linked low neutrophil activation to efficient mucin surface-shielding. Interestingly, the shielding power appeared equal for thick expanded and thin compact mucin coatings. Combined mucin-serum coatings were found to be highly surface-passivating. Particularly, since our data suggested partly synergistic mucin-serum action, we highlight the possibility that pre-adsorbed mucins could provide favorable support for adsorbing host components.

  • 189.
    Sandberg, Tomas
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Carlsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Karlsson Ott, Marjam
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Mucin coatings suppress neutrophil adhesion to a polymeric model biomaterial2007In: Microscopy research and technique (Print), ISSN 1059-910X, E-ISSN 1097-0029, Vol. 70, no 10, p. 864-868Article in journal (Refereed)
    Abstract [en]

    Following our recent study on the fractionation, characterization, and model adsorption of mucins derived from bovine salivary glands (BSM), porcine stomach scrapings (PGM), and human whole saliva (MG1), we here present a microscopic evaluation of the interactions between mucin-coated substrates and human neutrophils. Our results show that surface-coating with BSM, PGM, and MG1 can be effectively used to suppress the adhesion of neutrophils to a polymeric model biomaterial (Thermanox). Neutrophil morphologies found on Thermanox substrates coated with mucins resemble those observed for nonactivated neutrophils found in circulation. Notably, low neutrophil adhesion can be obtained at a significantly lower coating concentration (0.125 mg/mL) for the compositionally complex MG1 mucin than for the relatively pure BSM and PGM mucins (1 mg/mL). Furthermore, since coating at a low BSM and PGM concentration (0.25 mg/mL) results in higher cell counts and more spread cells than in the high-concentration case, we suggest that dense mucin surface packing is critical for good coating performance. In conclusion, the present study demonstrates how mucins from three different sources, of different compositional and structural status, efficiently can be used to suppress neutrophil adhesion and activation. This finding makes them potent candidates for use as biomaterial coatings.

  • 190.
    S.-C. Huang, K.D. Caldwell, J.-N. Lin, and J.N. Herron
    Uppsala University, Centre for Surface Biotechnology.
    Site-Specific Immobilization of Monoclonal Antibodies using Spacer-Mediated Antibody Attachment1996In: Langmuir, Vol. 12, p. 4292-4298Article in journal (Refereed)
  • 191.
    S.-C. Huang, M.D. Stump, R. Weiss, and K.D. Caldwell
    Uppsala University, Centre for Surface Biotechnology.
    Binding of Biotinylated DNA to Streptavidin-Coated Polystyrene Latex: Effects of Chain Length and Particle Size1996In: Anal. Biochem., Vol. 237, p. 115-122Article in journal (Refereed)
  • 192.
    Schulz, A
    et al.
    Uppsala University, Centre for Surface Biotechnology.
    Rex, M
    Harris, NRP
    Braathern, GO
    Reimer, E
    Alfier, R
    Kilbane-Dawe, I
    Eckermann, S
    Allaart, M
    Alpers, M
    Bojkov, B
    Cisneros, J
    Claude, H
    Cuevas, E
    Davies, J
    De, Backer H
    Dier, H
    Dorokhov, V
    Fast, H
    Godin, S
    Johnson, B
    Kois, B
    Kondo, Y
    Kosmidis, E
    Arctic ozone loss in threshold conditions: Match observations in 1997/1998 and 1998/19992001In: JOURNAL OF GEOPHYSICAL RESEARCH-ATMOSPHERES, ISSN 0747-7309, Vol. 106, no D7, p. 7495-7503Article in journal (Refereed)
    Abstract [en]

    Chemical ozone loss rates inside the Arctic polar vortex were determined in early 1998 and early 1999 by using the Match technique based on coordinated ozonesonde measurements. These two winters provide the only opportunities in recent years to investigat

  • 193.
    Shi, L
    et al.
    Uppsala University, Centre for Surface Biotechnology.
    Ardehali, R
    Caldwell, K.D
    Valint, P
    Mucin Coating on Polymeric Material Surfaces to Suppress Bacterial Adhesion2000In: Colloids and Surfaces B:Biointerfaces, Vol. 17, p. 229-239Article in journal (Refereed)
  • 194.
    Shi, L
    et al.
    Uppsala University, Centre for Surface Biotechnology.
    Caldwell, K.D
    Mucin Adsorption to Hydrophobic Surfaces2000In: J. Coll. Interface Sci., Vol. 224, p. 372-381Article in journal (Refereed)
  • 195.
    Shi, L
    et al.
    Uppsala University, Centre for Surface Biotechnology.
    Miller, C
    Caldwell, K.D
    Valint, P
    Effects of Mucin Addition on the Stability of Oil-Water Emulsions1999In: Colloids and Surfaces B:Biointerfaces, Vol. 15, p. 303-312Article in journal (Refereed)
  • 196.
    Shi, Lei
    et al.
    Uppsala University, Centre for Surface Biotechnology.
    Ardehali, Reza
    Valint, Paul
    Caldwell, Karin D
    Bacterial adhesion to model surface with self-generated protection coating of mucin via jacalin2001Article in journal (Refereed)
  • 197.
    Smith, M. P., Bulmer, M., Hjorth, R., and Titchener-Hooker, N. J.
    Uppsala University, Centre for Surface Biotechnology.
    A comparative engineering study of the use of expanded bed and packed bed routes for the recovery of labile proteins from crude feedstocks1996In: 5th World Congress of Chemical Engineering (San Diego), 1996, p. 565-570Conference paper (Other scientific)
  • 198.
    Stadejek T., Vilcek S., Lowings J.P., Ballagi-Pordany, A., Paton, D.J. and Belak, S.
    Uppsala University, Centre for Surface Biotechnology.
    Genetic heterogeneity of classical swine fever virus in Central Europe1997In: Virus Res, Vol. 52, no 2, p. 195-204Article in journal (Refereed)
  • 199.
    Stewart, R.
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology, Centre for Surface Biotechnology.
    Caldwell, K.D.
    Ho, C.H.
    Limberis, L.
    Metal-Chelating Surfactant2000Patent (Other (popular scientific, debate etc.))
  • 200.
    Tan, J.S., Harrison, C.A., Li, J.-T. and Caldwell, K.D.
    Uppsala University, Centre for Surface Biotechnology.
    Characterization of Soluble Polyelectrolyte-Gelatin Complexes by Differential Size Exclusion Chromatography and Flow Field-Flow Fractionation1998In: J. Polymer Sci : Part B: Polymer Physics, Vol. 36, p. 537-542Article in journal (Refereed)
12345 151 - 200 of 234
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