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  • 1.
    Burestedt, E.
    et al.
    Department of Analytical Chemistry, University of Lund, Lund, Sweden.
    Emnéus, J.
    Department of Analytical Chemistry, University of Lund, Lund, Sweden.
    Gorton, L.
    Department of Analytical Chemistry, University of Lund, Lund, Sweden.
    Marko-Varga, G.
    Department of Analytical Chemistry, University of Lund, Lund, Sweden.
    Domínguez, E.
    Department of Analytical Chemistry, Faculty of Pharmacy, University of Alcalá de Henares, Alcalá de Henares, Spain.
    Ortega, F.
    Department of Analytical Chemistry, Faculty of Pharmacy, University of Alcalá de Henares, Alcalá de Henares, Spain.
    Narváez, A.
    Department of Analytical Chemistry, Faculty of Pharmacy, University of Alcalá de Henares, Alcalá de Henares, Spain.
    Irth, H.
    Division of Analytical Chemistry, Leiden/Amsterdam Center for Drug Research, Leiden, The Netherlands.
    Lutz, Mareike
    Division of Analytical Chemistry, Leiden/Amsterdam Center for Drug Research, Leiden, The Netherlands.
    Puig, D.
    Department of Environmental Chemistry, CID-CSIC, Barcelona, Spain.
    Barceló, D.
    Department of Environmental Chemistry, CID-CSIC, Barcelona, Spain.
    Optimisation and validation of an automated solid phase extraction technique coupled on-line to enzyme-based biosensor detection for the determination of phenolic compounds in surface water samples1995Inngår i: Chromatographia, ISSN 0009-5893, E-ISSN 1612-1112, Vol. 41, nr 3-4, s. 207-215Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    A fully integrated screening system for phenolic compounds was developed incorporating on-line solid phase extraction, fractionation and biosensor detection. Two different types of biosensors, solid graphite and carbon paste electrodes incorporating the enzyme tyrosinase, were compared and used in the screening system. Interfacing of the solid phase extraction and fractionation with the biosensor detection was given special attention since the biosensors were not compatible with the organic modifier used for desorption of phenols from the solid phase extraction step. The system was validated with conventional analytical techniques. Surface water samples from the Ebro river were spiked with 1,10, and 25μg L−1 of catechol, phenol,p-cresol, respectively. Three out of seven samples were spiked and the correct samples were identified, containing phenols equivalent to the spiked concentrations. © 1995 Friedr. Vieweg & Sohn Verlagsgesellschaft mbH.

  • 2.
    Jogbratt, Arvid
    Högskolan i Halmstad, Sektionen för ekonomi och teknik (SET).
    Kadmium som begränsande faktor för användande av tång som biogassubstrat - en laborativ undersökning:  2011Independent thesis Basic level (degree of Bachelor), 10 poäng / 15 hpOppgave
    Abstract [sv]

    Sveriges miljömål ”Begränsad klimatpåverkan” beskriver ambitionen att fram till år 2020 ska ha minskat utsläppen av växthusgaser med 40 % gentemot år 1990. Ett sätt för Sverige att lyckas med de uppsatta målen är att utveckla biogasproduktionen. Potentialen för biogasproduktion bedöms vara mycket stor och forskning för att ta fram nya substrat att använda inom biogasframställningen pågår. Ett möjligt substrat är alger, dock har tidigare forskning påvisat höga kadmiumhalter i alger vilket kan innebära problem för spridning av rötresten.  

       Syftet med denna rapport var att  genom laborativ och litterär undersökning bedöma algers potential som biogassubstrat och gödningsmedel.

       Resultaten påvisade höga kadmiumkoncentrationer hos alger vilket försvårar en spridning av kadmium till åkermark. De framtagna gränsvärdena för kadmiuminnehåll hos gödningsmedel överskrids för samtliga prover. Det ringa gödningsvärdet hos rötresten grundas i det låga fosforinnehållet hos algerna. Gaspotentialen för rötning av alger med organiskt avfall visade sig vara mycket god, vilket kan motivera en utveckling av effektiva, billiga, reningsmetoder för kadmium. För Halmstad kommun beräknades energiproduktionen av alger att vara av betydelse om ytterligare utveckling av uppsamling och skörd utreds.

       Metoder för kadmiumavskiljning har studerats och i Japan har en effektiv reningsmetod som baseras på urlakning följt av adsorption med naturliga koaguleringsmedel framställda från fruktavfall tagits fram. Andra metoder som möjliggör rötning av alger är att kombinera biogasframställning med produktion av energiskog. Odlingarna kan gödslas med den kadmiumrika rötresten, varefter den skördade energiskogen förbränns och renas från kadmium på förbränningsanläggning.

  • 3.
    Larsson, Marita
    et al.
    DMPK and Bioanalytical Chemistry, AstraZeneca R&D Mölndal, Mölndal, Sweden.
    Lutz, Mareike
    DMPK and Bioanalytical Chemistry, AstraZeneca R&D Mölndal, Mölndal, Sweden.
    Transient isotachophoresis for sensitivity enhancement in capillary electrophoresis-mass spectrometry for peptide analysis2000Inngår i: Electrophoresis, ISSN 0173-0835, E-ISSN 1522-2683, Vol. 21, nr 14, s. 2859-2865Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Transient isotachophoresic (ITP) focusing was used for the on-line analysis of peptides by capillary zone electrophoresis-mass spectrometry (CZE-MS), allowing injection volumes of up to 0.9 microL. A sheath liquid electrospray interface was used with a single quadrupole mass analyzer. First, the technique was applied to the qualitative analysis of a tryptic digest of cytochrome c, resulting in low-background, high-quality spectra. Second, the linear range was investigated by selected ion monitoring (SIM) for a peptidomimetic direct thrombin inhibitor melagatran (Mr 429.5) and two endogenous peptides, substance P (Mr 1348) and calcitonin gene-related peptide (alpha-CGRP; Mr 3806).

  • 4.
    Lutz, Mareike
    et al.
    Division of Analytical Chemistry, Leiden/Amsterdam Center for Drug Research, Leiden, Netherlands.
    Burestedt, Elisabeth
    Department of Analytical Chemistry, University of Lund, Lund, Sweden.
    Emnéus, Jenny
    Department of Analytical Chemistry, University of Lund, Lund, Sweden.
    Lidén, Helena
    Department of Analytical Chemistry, University of Lund, Lund, Sweden.
    Gobhadi, Shahpar
    Department of Analytical Chemistry, University of Lund, Lund, Sweden.
    Gorton, Lo
    Department of Analytical Chemistry, University of Lund, Lund, Sweden.
    Marko-Varga, György
    Department of Analytical Chemistry, University of Lund, Lund, Sweden.
    Effects of different additives on a tyrosinase based carbon paste electrode1995Inngår i: Analytica Chimica Acta, ISSN 0003-2670, E-ISSN 1873-4324, Vol. 305, nr 1-3, s. 8-17Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    The influence of a number of solid and chemical additives on the sensitivity and operational stability of a tyrosinase carbon paste electrode was studied. Cyclic voltammograms were run of the electrochemically active catechol/o-quinone couple on unmodified and additive modified carbon paste electrodes without tyrosinase. This was done in order to study the influence of these additives on the pure electrochemistry of the carbon paste. The influence on the total system (additive and enzyme modified carbon paste electrode) was studied in the flow injection mode. In some instances a dramatic improvement of the direct electron transfer of the catechol/o-quinone couple was obtained with both solid and chemical additives included in the carbon paste. A similar improvement of biosensor sensitivity in the flow injection mode was obtained with most chemical additives whereas the solid additives had a negative impact on biosensor sensitivity. The results obtained in this work indicate that these additives influence the purely electrochemical processes at the carbon paste and/or the performance of the enzyme in the carbon paste environment. How and why these additives can possibly influence the biosensor performance are discussed. © 1995.

  • 5.
    Lutz, Mareike
    et al.
    Division of Analytical Chemistry, Leiden/Amsterdam Center for Drug Research, Leiden University, Leiden, The Netherlands.
    Dominguez, Elena
    Department of Analytical Chemistry, Faculty of Pharmacy, University of Alcalá de Henares, Alcalá de Henares (Madrid), Spain.
    Development and Optimization of a Solid Composite Tyrosinase Biosensor for Phenol Detection in Flow Injection Systems1996Inngår i: Electroanalysis, ISSN 1040-0397, E-ISSN 1521-4109, Vol. 8, nr 2, s. 117-123Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Bulk-modified epoxy-graphite tyrosinase biosensors were fabricated by four different procedures. The influence of these fabrication procedures on the analytical performance of the enzyme electrode in an amperometric wall-jet flow cell has been studied. The bioprobe performance is assessed by cyclic voltammetry. Higher current densities and narrower peaks were obtained when the enzyme was introduced in the dry state into the epoxy-graphite material, instead of introducing it previously dissolved in the buffer. In the FI system responses of 11.79 μA cm-2 and 1.43 μA cm-2 are then obtained for catechol and phenol respectively for 50 μL injections of 20 μM solutions. Moreover, if gold/palladium is introduced into the epoxy-graphite, a further increase in current is achieved resulting in 27.70 μA cm-2 and 4.90 μA cm-2 for catechol and phenol, respectively. This biosensor can operate in aqueous as well as in mixed aqueous-organic environments.

  • 6.
    Lutz, Mareike
    et al.
    Division of Analytical Chemistry, Leiden/Amsterdam Center for Drug Research, Leiden University, Leiden, The Netherlands.
    Irth, Hubertus
    Division of Analytical Chemistry, Leiden/Amsterdam Center for Drug Research, Leiden University, Leiden, The Netherlands.
    Tjaden, Ubbo R.
    Division of Analytical Chemistry, Leiden/Amsterdam Center for Drug Research, Leiden University, Leiden, The Netherlands.
    van der Greef, Jan
    Division of Analytical Chemistry, Leiden/Amsterdam Center for Drug Research, Leiden University, Leiden, The Netherlands.
    Applying hollow fibres for separating free and bound label in continuous-flow immunochemical detection1996Inngår i: Journal of Chromatography A, ISSN 0021-9673, E-ISSN 1873-3778, Vol. 755, nr 2, s. 179-187Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    On-line liquid chromatography-immunochemical detection (LC-ICD) provides the possibility to individually monitor cross-reactive compounds overcoming the need of tedious fraction collection. ICD is performed as a post-column reaction detection system and is based on a two-step immunoreaction. In the first step unlabelled antibodies are added to the LC effluent and allowed to react with antigens (analytes) eluting from the LC column. The amount of analytes bound to the antibodies is measured by adding, in a second step, labelled antigen to the reaction mixture. For quantitation, free and bound label need to be separated prior to detection. The present paper describes a hollow fibre module (HFM), which can be used for this purpose. Separation of free and bound label occurs on discrimination by size. Using biotin as a model compound, a detection limit of 30 nmol/l can be reached employing anti-biotin antibodies and a low-molecular-mass fluorescence label in the LC-ICD system. Additional to low-molecular-mass labels, the HFM allows the use of small enzyme labels. In this context, horseradish peroxidase-labelled biotin was used as a label in combination with antibodies in the immunochemical detection of biotin. This allows future implementation of commercially available enzyme immunoassay kits in continuous-flow immunochemical detection.

  • 7.
    Lutz, Mareike
    et al.
    Division of Analytical Chemistry, Leiden/Amsterdam Center for Drug Research, Leiden University, Leiden, The Netherlands.
    Irth, Hubertus
    Division of Analytical Chemistry, Leiden/Amsterdam Center for Drug Research, Leiden University, Leiden, The Netherlands.
    Tjaden, Ubbo R.
    Division of Analytical Chemistry, Leiden/Amsterdam Center for Drug Research, Leiden University, Leiden, The Netherlands.
    van der Greef, Jan
    Division of Analytical Chemistry, Leiden/Amsterdam Center for Drug Research, Leiden University, Leiden, The Netherlands.
    Biochemical detection for direct bead surface analysis1997Inngår i: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 69, nr 23, s. 4878-4884Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    A continuous-now biochemical detection system is presented which recognizes biologically active compounds immobilized to solid phases. This approach can be used to screen, for example, solid-phase combinatorial libraries for lead compounds. Biochemical detection is performed by mixing a plug of a solid-phase suspension with labeled affinity protein, During a short reaction time, the labeled affinity protein will only bind to ligands, i.e., compounds with biological activity. Hereafter, the free and bound labels are separated by means of a hollow fiber module, Quantitation of the free label is performed with a conventional now-through fluorescence detector, Total assay time amounts to less than 3 min. Biochemical detection for direct bead surface analysis was developed for two model systems. The first model system used fluorescence-labeled avidin as affinity protein and its ligands biotin and iminobiotin immobilized to agarose as analytes. The second model system used fluorescence-labeled antisheep (Fab)(2) fragments as affinity protein and different IgGs immobilized to agarose as analytes. The feasibility of this approach for recognition of solid-phase immobilized ligands was documented by screening 50 samples with a 100% hit rate.

  • 8.
    Lutz, Mareike
    et al.
    Division of Analytical Chemistry, Leiden/Amsterdam Center for Drug Research, Leiden University, Leiden, Netherlands.
    Irth, Hubertus
    Division of Analytical Chemistry, Leiden/Amsterdam Center for Drug Research, Leiden University, Leiden, Netherlands.
    Tjaden, Ubbo R.
    Division of Analytical Chemistry, Leiden/Amsterdam Center for Drug Research, Leiden University, Leiden, Netherlands.
    van der Greef, Jan
    Division of Analytical Chemistry, Leiden/Amsterdam Center for Drug Research, Leiden University, Leiden, Netherlands.
    Implementation of affinity solid-phases in continuous-flow biochemical detection1997Inngår i: Journal of Chromatography A, ISSN 0021-9673, E-ISSN 1873-3778, Vol. 776, nr 2, s. 169-178Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    A continuous-flow biochemical detection system is presented which allows the use of solid-phase immobilised affinity proteins. The biochemical detection is performed by mixing analyte with a labelled ligand followed by the addition of solid-phase immobilised affinity protein. After a reaction time of 85 s, free and bound label are separated by means of a hollow fibre module. Quantitation of the free label is performed with a conventional flow-through fluorescence detector. Total assay time amounts to less than 2 min. Biotin was chosen as the model compound using a range of streptavidin-coated solid-phases and an antibody-coated solid-phase as affinity material, and fluorescein–biotin as low-molecular-mass label. The relative standard deviation for twenty repetitive injections was 10.9%. A calibration curve was constructed in the concentration range between 20 and 400 nmol l−1 leading to a correlation coefficient of 0.994. A limit of detection of 8 nmol l−1 was obtained. © 1997 Elsevier Science B.V.

  • 9.
    Lutz, Mareike
    et al.
    Bioanalytical Chemistry, Astra Hässle AB, Mölndal, Sweden.
    Larsson, Marita
    Bioanalytical Chemistry, Astra Hässle AB, Mölndal, Sweden.
    On-Line Microdialysis-Electrospray Mass Spectrometry for Automated Desalting of Small-Volume Peptide Samples1999Inngår i: Chromatographia, ISSN 0009-5893, E-ISSN 1612-1112, Vol. 49, nr Suppl. 1, s. S28-S34Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Electrospray ionization mass spectrometry (ESI-MS) is an important tool for biomolecule analysis. Because the salt content of small-volume peptide samples can hamper analyte ionization, such samples require treatment before ESI-MS.The approach described here consists in interfacing ESI-MS with on-line microdialysis which affords rapid desalting and buffer-exchange. On-line microdialysis was performed by means of a hollow fiber (i.d. 200 μm) coupled to fused silica capillaries. Peptide samples were introduced into the capillary flow system as plugs and transferred to the dialysis cell and the electrospray by means of hydrodynamic pressure. As a result, the ionization efficiency of peptidic analytes was increased and adduct formation with, e.g., sodium, was reduced owing to reduced levels of nonvolatile salts. The feasibility of on-line microdialysis-ESI-MS is shown with a proteolytic digest originating from two-dimensional gel electrophoresis.

  • 10.
    Lutz, Mareike
    et al.
    DMPK & Bioanalytical Chemistry, AstraZeneca R&D Mölndal, Mölndal, Sweden.
    Markling, Magnus E.
    DMPK & Bioanalytical Chemistry, AstraZeneca R&D Mölndal, Mölndal, Sweden.
    Masimirembwa, Collen M.
    DMPK & Bioanalytical Chemistry, AstraZeneca R&D Mölndal, Mölndal, Sweden.
    Monolithic silica rod liquid chromatography with ultraviolet or fluorescence detection for metabolite analysis of cytochrome P450 marker reactions2002Inngår i: Journal of chromatography. B, ISSN 1570-0232, E-ISSN 1873-376X, Vol. 780, nr 2, s. 205-215Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    In vitro cytochrome P450 assays are used in metabolism studies in support of early phases of drug discovery to investigate, e.g., metabolic stability, enzyme inhibition and induction by new chemical entities. LC-UV and LC-fluorescence are traditional analytical tools in support of such studies. However, these tools typically comprise different methods of relatively low throughput for the various metabolites of probe reactions. In recent years, LC-MS methods have been developed to increase throughput. Increased throughput can also be achieved by means of modern chromatographic tools in combination with UV and fluorescence detection. This approach is especially suitable when cytochrome P450 isoforms are investigated by means of single probe incubations. Here, an LC-UV/fluorescence system based on a monolithic porous silica column is described for the analysis of metabolites of nine cytochrome P450 marker reactions [phenacetin to paracetamol (CYP1A2), coumarin to 7-hydroxycoumarin (CYP2A6), paclitaxel to 6alpha-hydroxypaclitaxel (CYP2C8), diclofenac to 4-hydroxydiclofenac (CYP2C9), mephenytoin to 4-hydroxymephenytoin (CYP2C19), bufuralol to 1-hydroxybufuralol (CYP2D6), chlorzoxazone to 6-hydroxychlorzoxazone (CYP2E1), midazolam to 1-hydroxymidazolam (CYP3A4), and testosteron to 6beta-hydroxytestosteron (CYP3A4)]. While offering sensitivities and linear ranges comparable to previously reported methods, the set-up described here provides ease of use and increased throughput with maximum cycle times of 4.5 min. © 2002 Elsevier Science B.V. All rights reserved.

  • 11.
    Lutz, Mareike
    et al.
    Division of Analytical Chemistry, Leiden/Amsterdam Ctr. for Drug Res., Leiden University, Leiden, Netherlands.
    Oosterkamp, Aaike J.
    Division of Analytical Chemistry, Leiden/Amsterdam Ctr. for Drug Res., Leiden University, Leiden, Netherlands.
    Irth, Hubertus
    Division of Analytical Chemistry, Leiden/Amsterdam Ctr. for Drug Res., Leiden University, Leiden, Netherlands.
    On-line Coupling of Liquid Chromatography to Biological Assays1997Inngår i: Chimica oggi, ISSN 0392-839X, E-ISSN 1973-8250, Vol. 15, nr 1-2, s. 11-15Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    Combining two powerful technologies - liquid chromatography and bioassays results in analytical methodologies which are characterised by high selectivity and sensitivity. In contrast to microtitre-type bioassays, biochemical reactions proceed in a closed, continuous-flow reaction detection system coupled directly to the outlet of the chromatographic separation column. The interaction of substances eluting from the separation column with molecular targets such as antibodies or receptors is monitored directly overcoming tedious fraction collection and manual operations required to prepare the functions for batch immunoassays. important application areas are bioanalysis and drug discovery.

  • 12.
    Marko-Varga, György
    et al.
    Department of Analytical Chemistry, Lund University, Lund, Sweden.
    Burestedt, Elisabeth
    Department of Analytical Chemistry, Lund University, Lund, Sweden.
    Svensson, Carl Johan
    Department of Analytical Chemistry, Lund University, Lund, Sweden.
    Emnéus, Jenny
    Department of Analytical Chemistry, Lund University, Lund, Sweden.
    Gorton, Lo
    Department of Analytical Chemistry, Lund University, Lund, Sweden.
    Ruzgas, Tautgirdas
    Enzyme Chemistry Laboratory, Institute of Biochemistry, Vilnius, Lithuania.
    Lutz, Mareike
    Division of Analytical Chemistry, Leiden/Amsterdam Center for Drug Research, Leiden, The Netherlands.
    Unger, Klaus K.
    Institute für Anorganische Chemie und Analytische Chemie, Johannes Gutenberg-Universität, Mainz, Germany.
    Effect of HY-Zeolites on the Performance of Tyrosinase-Modified Carbon Paste Electrodes1996Inngår i: Electroanalysis, ISSN 1040-0397, E-ISSN 1521-4109, Vol. 8, nr 12, s. 1121-1126Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    The dependence of electrode response on additive properties in enzyme-modified carbon paste was studied. Four different HY-zeolite powders, dealuminated to different extents and characterized by both Si/Al ratio and hydrophilicity, were used as the carbon paste modifiers. The enzyme tyrosinase used in biosensors for the detection of catechol and other phenolic compounds was chosen as the model system for the construction of a composite carbon paste biosensor incorporating different HY-zeolites as additives. Tyrosinase was trapped on the HY-zeolite particles from a buffer solution, dried and mixed with graphite powder and a pasting oil. It was found that by incorporating HY-zeolites into the carbon paste the heterogeneous reaction rate of catechol redox conversion and the signal response for catechol were increased. In the latter case a higher response was observed for increased hydrophilicity, i.e., decreased Si/Al ratio of the HY-zeolite. The carbon paste/solution interface is considered to be an aqueous/organic phase and the characteristics of the enzyme-modified carbon paste electrode are related to theories, explaining enzymatic catalysis in organic solvents.

  • 13.
    Monaghan, T.
    et al.
    Wolfson School of Mechanical and Manufacturing Engineering, Loughborough University, Ashby Road, Loughborough, United Kingdom.
    Harding, M. J.
    Department of Chemistry, Loughborough University, Epinal Way, Loughborough, United Kingdom.
    Harris, R. A.
    School of Mechanical Engineering, University of Leeds, Leeds, United Kingdom.
    Friel, R. J.
    Wolfson School of Mechanical and Manufacturing Engineering, Loughborough University, Ashby Road, Loughborough, United Kingdom.
    Christie, S. D. R.
    Department of Chemistry, Loughborough University, Epinal Way, Loughborough, United Kingdom.
    Customisable 3D printed microfluidics for integrated analysis and optimisation2016Inngår i: Lab on a Chip, ISSN 1473-0197, E-ISSN 1473-0189, Vol. 16, nr 17, s. 3362-3373Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    The formation of smart Lab-on-a-Chip (LOC) devices featuring integrated sensing optics is currently hindered by convoluted and expensive manufacturing procedures. In this work, a series of 3D-printed LOC devices were designed and manufactured via stereolithography (SL) in a matter of hours. The spectroscopic performance of a variety of optical fibre combinations were tested, and the optimum path length for performing Ultraviolet-visible (UV-vis) spectroscopy determined. The information gained in these trials was then used in a reaction optimisation for the formation of carvone semicarbazone. The production of high resolution surface channels (100–500 μm) means that these devices were capable of handling a wide range of concentrations (9 μM–38 mM), and are ideally suited to both analyte detection and process optimisation. This ability to tailor the chip design and its integrated features as a direct result of the reaction being assessed, at such a low time and cost penalty greatly increases the user's ability to optimise both their device and reaction. As a result of the information gained in this investigation, we are able to report the first instance of a 3D-printed LOC device with fully integrated, in-line monitoring capabilities via the use of embedded optical fibres capable of performing UV-vis spectroscopy directly inside micro channels. © The Royal Society of Chemistry 2016.

  • 14.
    Owens, Paul K.
    et al.
    Analytical Chemistry, Pharmaceutical R&D, Astra Hässle AB, Mölndal, Sweden.
    Karlsson, Lars
    Analytical Chemistry, Pharmaceutical R&D, Astra Hässle AB, Mölndal, Sweden.
    Lutz, Mareike
    Bioanalytical Chemistry, Astra Hässle AB, Mölndal, Sweden.
    Andersson, Lars I.
    Bioanalytical Chemistry, Concept Division, Astra Pain Control AB, Södertälje, Sweden.
    Molecular imprinting for bio- and pharmaceutical analysis1999Inngår i: TrAC. Trends in analytical chemistry, ISSN 0165-9936, E-ISSN 1879-3142, Vol. 18, nr 3, s. 146-154Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    The potential of analytical techniques based on molecular imprinting is reviewed from the viewpoint of bio- and pharmaceutical analysis. A literature study shows that molecularly imprinted polymers (MIPs) have been implemented predominantly in three areas of interest to pharmaceutical industry laboratories. First, in sample preparation, imprinted polymers are used as the sorbent for solid phase extraction purposes. Secondly, MIPs serve as the stationary phase for analytical chromatographic and electrophoretic separations. Thirdly, imprinted polymers are utilised as analyte recognition materials in affinity assays. The advantages of MIPs, e.g., physical robustness, high strength, resistance to elevated temperatures and pressures, and inertness towards acids, bases, metal ions and organic solvents, have been well exploited in a large number of applications. This article focuses on how these benefits may be used for improving the quality of analytical procedures. Some key MIP disadvantages are also highlighted, especially in relation to other analytical techniques. (C) 1999 Published by Elsevier Science B.V. All rights reserved.

  • 15.
    Pobric, Dzenana
    Högskolan i Halmstad, Akademin för lärande, humaniora och samhälle.
    DNA-analys och idemtifikation: En studie om olika metoder för DNA-analys som används för identifikation av mänskliga skelettdelar2018Independent thesis Basic level (professional degree), 10 poäng / 15 hpOppgave
  • 16.
    Račaitytė, Kristina
    et al.
    Kaunas University of Technology, Department of Organic Technology, Kaunas, Lithuania.
    Lutz, Mareike
    Bioanalytical Chemistry, AstraZeneca R&D Mölndal, Mölndal, Sweden.
    Unger, Klaus K.
    Institut für Anorganische Chemie und Analytische Chemie, Johannes Gutenberg Universität, Mainz, Germany.
    Lubda, Dieter
    Merck KGaA, Specialty Laboratory Products, Darmstadt, Germany.
    Boos, Karl Siegfried
    Klinikum Grosshadern, Institut für Klinische Chemie, Munich, Germany.
    Analysis of neuropeptide Y and its metabolites by high-performance liquid chromatography–electrospray ionization mass spectrometry and integrated sample clean-up with a novel restricted-access sulphonic acid cation exchanger2000Inngår i: Journal of Chromatography A, ISSN 0021-9673, E-ISSN 1873-3778, Vol. 890, nr 1, s. 135-144Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    A novel restricted access cation exchanger with sulphonic acid groups at the internal surface was proven to be highly suitable in the sample clean up of peptides on-line coupled to HPLC–electrospray ionization (ESI)-MS. Neuropeptide Y (NPY) and several of its fragments in plasma were subjected to the sample clean-up procedure. The peptides were eluted by a step gradient from the restricted access column, applying 10 mM phosphate buffer pH 3.5 from 5 to 20% (v/v) of acetonitrile with 1 M NaCl and transferred to a Micra ODS II column (33×4.6 mm). The separation of the peptides and their fragments was performed by a linear gradient from 20 to 60% (v/v) acetonitrile in water with 0.1% formic acid and 0.01% trifluoroacetic acid in 4 min at a flow-rate of 0.75 ml/min. An integrated and completely automated system composed of sample clean up–HPLC–ESI-MS was used to analyze real life samples. The sample volumes ranged between 20 and 100 μl. Peaks due to the fragments NPY 1–36, 3–36 and 13–36 in porcine plasma were identified by ESI-MS. The limit of detection was in the 5 nmol/ml range. The total analysis required 21 min and allowed the direct injection of plasma. © 2000 Elsevier Science B.V. All rights

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