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  • 101.
    Hjorth, R.
    Uppsala University, Centre for Surface Biotechnology.
    Expanded-bed adsorption in industrial bioprocessing: recent developments1997In: Trends in biotechnology, Vol. 15, p. 230-235Article in journal (Refereed)
  • 102.
    Hjorth, R., Kämpe, S., and Carlsson, M.
    Uppsala University, Centre for Surface Biotechnology.
    Analysis of some operating parameters of novel adsorbents for recovery of proteins in expanded beds1995In: Bioseparation, Vol. 5, p. 217-223Article in journal (Refereed)
  • 103.
    Hjorth, R., Leijon, P., Barnfield-Frej, A.-K., and Jägersten, C.
    Uppsala University, Centre for Surface Biotechnology.
    Expanded bed adsorption chromatography1998In: G. Subramanian, (ed.), Bioseparation and Bioprocessing, Wiley-VCH, Weinheim , 1998, p. 199-226Chapter in book (Other scientific)
  • 104.
    Ho, C.-H., Limberis, L., Caldwell, K.D., and Stewart, R.J.
    Uppsala University, Centre for Surface Biotechnology.
    A Metal-Chelating Pluronic for Immobilization of Histidine-Tagged Proteins at Interfaces: Immobilization of Firefly Luciferase on Polystyrene Beads1998In: Langmuir, Vol. 14, p. 3889-3894Article in journal (Refereed)
  • 105.
    Huang, Shao-Chie
    et al.
    Uppsala University, Centre for Surface Biotechnology.
    Tresco, Patrick A.
    Caldwell, Karin D.
    Structural integrity in protein immobilization.1997In: Polymer Preprints, The Division of PolymerChemistry, Inc.; American Chemical Society , 1997, Vol. 38, no 1, p. 561-562Conference paper (Other scientific)
  • 106.
    J. Carlsson, J.-C. Janson and M. Sparrman
    Uppsala University, Centre for Surface Biotechnology.
    Affinity Chromatography1998In: J.-C. Janson and L. Rydén, (eds.), Protein Purification, Principles, High Resolution Methods and Applications, John Wiley & Sons Inc., New York , 1998, p. 375-443Chapter in book (Other scientific)
  • 107.
    Janne, K
    et al.
    Uppsala University, Centre for Surface Biotechnology.
    Pettersen, J
    Lindberg, NO
    Lundstedt, T
    Medicinska vetenskapsområdet, Faculty of Pharmacy, Department of Medicinal Chemistry.
    Hierarchical principal component analysis (PCA) and projection to latent structure (PLS) technique on spectroscopic data as a data pretreatment for calibration2001In: JOURNAL OF CHEMOMETRICS, ISSN 0886-9383, Vol. 15, no 4, p. 203-213Article in journal (Refereed)
    Abstract [en]

    Spectroscopic data consists of several hundred to some thousand variables, wherein most of the variables are: autocorrelated. When PCA and PLS techniques are used for the interpretation of these kinds of data, the loading plots are usually complex due to

  • 108.
    Janson, Jan-Christer
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    L´histoire du développement du Sephadex2005In: LÓperon:: Bulletin de L´UPBM, Vol. 33, p. 2-11Article in journal (Refereed)
  • 109.
    Janson, Jan-Christer
    Uppsala University, Centre for Surface Biotechnology.
    Optimization of large-scale chromatography of proteins2001In: KOREAN JOURNAL OF CHEMICAL ENGINEERING, ISSN 0256-1115, Vol. 18, no 2, p. 149-158Article in journal (Refereed)
    Abstract [en]

    Protein chromatography is a very complex process based on a combination of thermodynamic, kinetic and mass transport phenomena. By virtue of their complicated and delicate surface structures, the behaviour of proteins on various chromatographic media is n

  • 110.
    Janson, Jan-Christer
    Uppsala University, Centre for Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    The Development of Gel Media and Columns for Large-Scale Chromatography of Proteins, a Historical Review2002In: Chinese J. Chem. Eng, Vol. 10, no 6, p. 690-695Article in journal (Refereed)
  • 111.
    Janson, Jan-Christer
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Jönsson, J. Å.
    Introduction to chromatography2011In: Protein Purification, Principles, High Resolution Methods and Applications / [ed] J-C Janson, John Wiley & Sons Inc. , 2011, 3, p. 25-50Chapter in book (Other academic)
  • 112.
    Jansson, Jan-Christer
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry. Ytbioteknik.
    Affinity 20052006In: Journal of Molecular Recognition, Vol. 19, no 4, p. 247-Article in journal (Refereed)
    Abstract [en]

    No abstract

  • 113.
    J.-C., Janson and J.-Å. Jönsson
    Uppsala University, Centre for Surface Biotechnology.
    Introduction to Chromatography1998In: J.-C. Janson and L. Rydén, (eds.), Protein Purification, Principles, High Resolution Methods and Applications, John Wiley & Sons Inc., New York , 1998, p. 43-78Chapter in book (Other scientific)
  • 114.
    Joerger, R
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Technology, Department of Materials Science. SOLID STATE PHYSICS.
    Klaus, T
    Centre for Surface Biotechnology.
    Granqvist, C.G.
    Functional Biomimetic Surface Coatings.2000In: The Annals of MCFA, Vol. 1, no 1, p. 39-44Article in journal (Refereed)
    Abstract [en]

    An interdisciplinary approach to materials science is proposed, involving biological methods that complement existing physical and chemical coating techniques. Silver-dielectric composite thin films were produced by a bio-logical technique, using microbia

  • 115.
    Joerger, R
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Technology, Department of Materials Science. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Technology, Department of Materials Science. SOLID STATE PHYSICS.
    Klaus, T
    Centre for Surface Biotechnology.
    Pettersson, J
    Chemistry, Department of Chemistry.
    Granqvist, C G
    Digestion method for silver accumulated in micro-organisms2000In: Fresenius J. Anal.Chem, Vol. 366, no 3, p. 311-312Article in journal (Refereed)
    Abstract [en]

    Silver is accumulated to high concentrations in certain microbial strains. Here a bomb digestion method is proposed, using HNO3 and HCl, for the extraction and digestion of silver and silver compounds from the organic matrix. The method is applicable for

  • 116.
    J.-T., Li and K.D. Caldwell
    Uppsala University, Centre for Surface Biotechnology.
    Plasma Protein Interactions with Pluronic™ Treated Colloids1996In: Colloids and Surfaces B: Biointerfaces, Vol. 7, p. 009-022Article in journal (Refereed)
  • 117.
    J.-T. Li, J. Carlsson, J.N. Lin, and K. D. Caldwell
    Uppsala University, Centre for Surface Biotechnology.
    Chemical Modification of Surface Active Poly(Ethylene Oxide)-Poly(Propylene Oxide) Triblock Copolymers1996In: Bioconjugate Chemistry, Vol. 7, p. 592-599Article in journal (Refereed)
  • 118.
    J.-T. Li, J. Carlsson, S.-C. Huang and K.D. Caldwell
    Uppsala University, Centre for Surface Biotechnology.
    Adsorption of Poly(ethylene oxide)-Containing Block Copolymers: A Route to Protein Resistance1996In: E. Glass, Ed., Hydrophilic Polymers, ACS Press, Washington , 1996, p. 61-78Chapter in book (Other scientific)
  • 119.
    Karlsson, M.
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Tang, L.
    Surface morphology and adsorbed proteins affect phagocyte responses to nano-porous alumina2006In: J Mater Sci: Mater Med, Vol. 17, p. 1101–1111-Article in journal (Refereed)
    Abstract [en]

    This study evaluates human neutrophil responses

    to aluminum oxide membranes with different pore sizes

    (20 nm and 200 nm in diameter) uncoated and pre-coated

    with serum, collagen I, or fibrinogen. The effect of released

    neutrophil granule components on the survival of osteoblastic

    cells (MG63) bound to the alumina membranes has also

    been evaluated.Without protein coatings the 20 nm pore-size

    membranes prompt higher reactive oxygen species (ROS)

    production as assessed by luminol-amplified chemiluminescence

    than the 200 nm pore-size membranes. Such pore-size

    depending responses were also found on membranes precoated

    with fibrinogen, but not with collagen or serum were

    in fact a much lower ROS production was observed. In addition,

    uncoated and fibrinogen-coated membranes prompt

    stronger release of the granule enzymes, myeloperoxidase

    and elastase, than collagen or serum-coated alumina. Equally

    important, we found that surface-mediated phagocyte activation

    and the subsequent release of granule components had a

    significant affect on the adhesion, viability and proliferation

    of osteoblasts. This stresses the importance of studying not

    only cell/surface interactions but also cell/cell interactions in

    wound healing and tissue regeneration processes.

  • 120.
    Karlsson, Marjam
    Uppsala University, Centre for Surface Biotechnology.
    Nano-pourus alumina, a potential bone implant coating (Mechanical properties and in vitro cell culture studies)2002Licentiate thesis, monograph (Other scientific)
  • 121.
    Karlsson, Marjam
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Surface Biotechnology.
    Pålsgård, Eva
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology, Centre for Surface Biotechnology.
    Wilshaw, Peter R
    Di Silvio, Lucy
    Initial in vitro interaction of osteoblasts with nano-porous alumina2003In: Biomaterials, ISSN 0142-9612, E-ISSN 1878-5905, Vol. 24, no 18, p. 3039-3046Article in journal (Refereed)
    Abstract [en]

    In the present study we have used a characterised primary human cell culture model to investigate cellular interactions with nano-porous alumina. This material, prepared by anodisation, is being developed as a coating on titanium alloy implants. The structure of the alumina, as determined by X-ray diffraction and transmission electron microscopy, was amorphous. When studying cell/material interactions we used both biochemical and morphological parameters. Cell viability, proliferation and phenotype were assessed by measurement of redox reactions in the cells, cellular DNA, tritiated thymidine ([H-3]-TdR) incorporation and alkaline phosphatase (ALP) production. Results showed a normal osteoblastic growth pattern with increasing cell numbers during the first 2 weeks. A peak in cell proliferation was seen on day 3, after which cell growth decreased, followed by an increase in ALP production, thus indicating that the osteoblastic phenotype was retained on the alumina. Cell adhesion was observed, the osteoblast-like cells having a flattened morphology with filipodia attached to the pores of the material. SDS-PAGE and western blot measurements showed that the nano-porous alumina was able to adsorb fibronectin. Trace amounts of aluminium ions were measured in the surrounding medium, but no adverse effect on cell activity was observed.

  • 122. Kaspereit, M.
    et al.
    Arnell, R.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Forssén, P.
    Seidel-Morgenstern, A.
    Fornstedt, Torgny
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Theoretische Analyse zum Einsatz von Additiven in der kontinuierlichen Chromatographie2008In: Chemie Ingenieur Technik, ISSN 0009-286X, E-ISSN 1522-2640, Vol. 80, no 9, p. 1305-1305Article in journal (Refereed)
  • 123.
    Klaus, T
    et al.
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Technology, Department of Materials Science. Centre for Surface Biotechnology. SOLID STATE PHYSICS.
    Joerger, R
    Olsson, E
    Granqvist, CG
    Silver-based crystalline nanoparticles, microbially fabricated1999In: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, ISSN 0027-8424, Vol. 96, no 24, p. 13611-13614Article in journal (Refereed)
    Abstract [en]

    One mechanism of silver resistance in microorganisms is accumulation of the metal ions in the cell. Here, we report on the phenomenon of biosynthesis of silver-based single crystals with well-defined compositions and shapes, such as equilateral trian

  • 124.
    Larsericsdotter, H
    et al.
    Uppsala University, Centre for Surface Biotechnology. IONPHYSICS.
    Oscarsson, S
    Teknisk-naturvetenskapliga vetenskapsområdet, Technology, Department of Materials Science.
    Buijs, J
    Thermodynamic analysis of proteins adsorbed on silica particles: Electrostatic effects2001In: JOURNAL OF COLLOID AND INTERFACE SCIENCE, ISSN 0021-9797, Vol. 237, no 1, p. 98-103Article in journal (Refereed)
    Abstract [en]

    Electrostatic effects on protein adsorption were investigated using differential scanning calorimetry (DSC) and adsorption isotherms, The thermal denaturation of lysozyme, ribonuclease A (RNase), and alpha -lactalbumin in solution and adsorbed onto silica

  • 125.
    Larsericsdotter, Helén
    Uppsala University, Centre for Surface Biotechnology.
    Macromolecules at Interfaces2004Doctoral thesis, comprehensive summary (Other academic)
    Abstract [en]

    In this thesis, the structure and stability of globular proteins adsorbed onto nanometer-sized hydrophilic silica particles were investigated using differential scanning calorimetry (DSC), hydrogen/deuterium exchange (HDX), and mass spectrometry (MS). The adsorption process itself was characterized with fluorescence and absorption spectroscopy and surface plasmon resonance (SPR). The combination of these methods offered a unique insight into adsorption-induced changes within proteins related to their adsorption characteristics. DSC contributed with thermodynamic information on the overall structural stability within the protein population. HDX in combination with MS contributed information on the structure and stability of adsorbed proteins with focus on changes within the secondary structure elements. In order to increase the structural resolution in this part of the investigation, proteolysis was performed prior to the MS analyzing step. Knowledge on the protein adsorption process was utilized in a practical approach called ligand fishing. In this approach, SPR was used to monitor the chip-based affinity purification of a protein with MS used for protein identification.

    Adsorption isotherms revealed that electrostatic interactions play an important role in the adsorption of proteins to hydrophilic surfaces. DSC investigation revealed that the thermal stability of proteins reduces with increasing electrostatic attraction between the protein and the surface and that this effect diminishes at higher surface coverage. The mass-increase due to exchange between protein hydrogen atoms and deuterium atoms in solution was investigated as a function of time. This gave insight into adsorption-induced changes in the structural stability of proteins. By combining DSC and HDX-MS, it was possible to differentiate between adsorption-induced changes in the secondary and tertiary structure. Additionally, if limited proteolysis was performed, the investigations gave insight into the orientation and protein segment specific changes in the stability of proteins adsorbed to silica surfaces. The adsorption of proteins to silica particles also provided the basis for a new experimental design that allows handling of minute amounts of proteins in a ligand fishing application, as used in the field of functional proteomics.

    List of papers
    1. Thermodynamic Analysis of Proteins Adsorbed on Silica Particles: Electrostatic Effects
    Open this publication in new window or tab >>Thermodynamic Analysis of Proteins Adsorbed on Silica Particles: Electrostatic Effects
    2001 In: Journal of Colloid and Interface Science, Vol. 237, no 1, p. 98-103Article in journal (Refereed) Published
    Identifiers
    urn:nbn:se:uu:diva-92363 (URN)
    Available from: 2004-11-17 Created: 2004-11-17Bibliographically approved
    2. Localized changes in the structural stability of myoglobin upon adsorption onto silica particles, as studied with hydrogen/deuterium exchange mass spectrometry
    Open this publication in new window or tab >>Localized changes in the structural stability of myoglobin upon adsorption onto silica particles, as studied with hydrogen/deuterium exchange mass spectrometry
    Show others...
    2003 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, Vol. 263, no 2, p. 441-448Article in journal (Refereed) Published
    National Category
    Natural Sciences
    Identifiers
    urn:nbn:se:uu:diva-92364 (URN)10.1016/S0021-9797(03)00401-6 (DOI)
    Available from: 2004-11-17 Created: 2004-11-17 Last updated: 2012-04-13Bibliographically approved
    3. Thermodynamic analysis of lysozyme adsorbed to silica
    Open this publication in new window or tab >>Thermodynamic analysis of lysozyme adsorbed to silica
    2004 In: Journal of Colloid and Interface Science, Vol. 276, no 2, p. 261-268Article in journal (Refereed) Published
    Identifiers
    urn:nbn:se:uu:diva-92365 (URN)
    Available from: 2004-11-17 Created: 2004-11-17Bibliographically approved
    4. Structure, Stability, and Orientation of BSA Adsorbed to Silica
    Open this publication in new window or tab >>Structure, Stability, and Orientation of BSA Adsorbed to Silica
    In: Journal of Colloid and Interface ScienceArticle in journal (Refereed) Submitted
    Identifiers
    urn:nbn:se:uu:diva-92366 (URN)
    Available from: 2004-11-17 Created: 2004-11-17Bibliographically approved
    5. Combining Surface Plasmon Resonance and Mass Spectrometry in Functional Proteomics: How to avoid and utilize non-specific adsorption
    Open this publication in new window or tab >>Combining Surface Plasmon Resonance and Mass Spectrometry in Functional Proteomics: How to avoid and utilize non-specific adsorption
    Show others...
    In: ProteomicsArticle in journal (Refereed) Submitted
    Identifiers
    urn:nbn:se:uu:diva-92367 (URN)
    Available from: 2004-11-17 Created: 2004-11-17Bibliographically approved
  • 126.
    Larsericsdotter, Helén
    et al.
    Uppsala University, Centre for Surface Biotechnology.
    Jansson, Östen
    Zhukov, Andrei
    Areskoug, Daphne
    Oscarsson, Sven
    Larsericsdotter, Helén
    Uppsala University, Centre for Surface Biotechnology.
    Combining Surface Plasmon Resonance and Mass Spectrometry in Functional Proteomics: How to avoid and utilize non-specific adsorptionIn: ProteomicsArticle in journal (Refereed)
  • 127.
    Larsericsdotter, Helén
    et al.
    Uppsala University, Centre for Surface Biotechnology.
    Oscarsson, Sven
    Buijs, Jos
    Structure, Stability, and Orientation of BSA Adsorbed to SilicaIn: Journal of Colloid and Interface ScienceArticle in journal (Refereed)
  • 128.
    Larsericsdotter, Helén
    et al.
    Uppsala University, Centre for Surface Biotechnology.
    Oscarsson, Sven
    Buijs, Jos
    Thermodynamic analysis of lysozyme adsorbed to silica2004In: Journal of Colloid and Interface Science, Vol. 276, no 2, p. 261-268Article in journal (Refereed)
  • 129.
    Larsericsdotter, Helén
    et al.
    Uppsala University, Centre for Surface Biotechnology.
    Oscarsson, Sven
    Buijs, Jos
    Thermodynamic Analysis of Proteins Adsorbed on Silica Particles: Electrostatic Effects2001In: Journal of Colloid and Interface Science, Vol. 237, no 1, p. 98-103Article in journal (Refereed)
  • 130.
    Larsson, Anna
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
    Anderson, Lars
    Xu, Bingze
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Muñoz, Inés
    Usòn, Isabel
    Janson, Jan-Christer
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Stålbrand, Henrik
    Ståhlberg, Jerry
    Three-dimensional crystal structure and enzymic characterization of beta-mannanase Man5A from blue mussel Mytilus edulis2006In: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 14, no 357, p. 1500-1510Article in journal (Refereed)
    Abstract [en]

    Endo-beta-1,4-d-mannanase is the key depolymerizing enzyme for beta-1,4-mannan polymers present in the cell walls of plants and some algae, as well as in some types of plant seeds. Endo-1,4-beta-mannanase from blue mussel Mytilus edulis (MeMan5A) belongs to the glycoside hydrolase (GH) family 5 enzymes. The MeMan5A structure has been determined to 1.6A resolution using the multiple-wavelength anomalous dispersion method at the selenium K edge with selenomethionyl MeMan5A expressed in the yeast Pichia pastoris. As expected for GH 5 enzymes, the structure showed a (betaalpha)(8)-barrel fold. An unusually large number of histidine side-chains are exposed on the surface, which may relate to its location within the crystalline style of the digestive tract of the mussel. Kinetic analysis of MeMan5A revealed that the enzyme requires at least six subsites for efficient hydrolysis. Mannotetraose (M4) and mannopentaose (M5) were shown to interact with subsites -3 to +1, and -3 to +2, respectively. A clear kinetic threshold was observed when going from M4 to M5, indicating that the +2 subsite provides important interaction in the hydrolysis of short oligomeric mannose substrates. The catalytic centre motif at subsite -1 found in superfamily GH clan A is, as expected, conserved in MeMan5A, but the architecture of the catalytic cleft differs significantly from other GH 5 enzyme structures. We therefore suggest that MeMan5A represents a new subfamily in GH 5.

  • 131.
    Larsson, Anna M.
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Anderson, Lars
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Xu, Bingze
    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. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry.
    Muñoz, Inés G.
    Usón, Isabel
    Janson, Jan-Christer
    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. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry.
    Stålbrand, Henrik
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry. Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Ståhlberg, Jerry
    Three-dimensional Crystal Structure and Enzymic Characterization of β-Mannanase Man5A from Blue Mussel Mytilus edulis2006In: Journal of Molecular Biology, Vol. 357, no 5, p. 1500-1510Article in journal (Refereed)
    Abstract [en]

    Endo-β-1,4-d-mannanase is the key depolymerizing enzyme for β-1,4-mannan polymers present in the cell walls of plants and some algae, as well as in some types of plant seeds. Endo-1,4-β-mannanase from blue mussel Mytilus edulis (MeMan5A) belongs to the glycoside hydrolase (GH) family 5 enzymes. The MeMan5A structure has been determined to 1.6 resolution using the multiple-wavelength anomalous dispersion method at the selenium K edge with selenomethionyl MeMan5A expressed in the yeast Pichia pastoris. As expected for GH 5 enzymes, the structure showed a (βα)8-barrel fold. An unusually large number of histidine side-chains are exposed on the surface, which may relate to its location within the crystalline style of the digestive tract of the mussel. Kinetic analysis of MeMan5A revealed that the enzyme requires at least six subsites for efficient hydrolysis. Mannotetraose (M4) and mannopentaose (M5) were shown to interact with subsites −3 to +1, and −3 to +2, respectively. A clear kinetic threshold was observed when going from M4 to M5, indicating that the +2 subsite provides important interaction in the hydrolysis of short oligomeric mannose substrates. The catalytic centre motif at subsite −1 found in superfamily GH clan A is, as expected, conserved in MeMan5A, but the architecture of the catalytic cleft differs significantly from other GH 5 enzyme structures. We therefore suggest that MeMan5A represents a new subfamily in GH 5.

  • 132.
    Ledung, G.
    et al.
    Uppsala University, Centre for Surface Biotechnology.
    Bergkvist, M.Quist, A.Gelius, U.Oscarsson, S.
    A Novel Method for Preparation of Highly reactive Disulphides on Silicon2001In: Proceedings 8th International Conference on Composite Engineering August 5-11, 2001, Tenerife, SpainConference proceedings (editor) (Other scientific)
  • 133. Li, Jing-Jing
    et al.
    Venkataramana, Musturi
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology. Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Sanyal, Suparna
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology. Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Janson, Jan-Christer
    Surface Biotechnology. Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Su, Zhi-Guo
    Immobilized β-cyclodextrin polymer coupled to agarose gel properly refolding recombinant Staphylococcus aureus elongation factor-G in combination with detergent micelle2006In: Protein Expression and Purification, Vol. 45, no 1, p. 72-79Article in journal (Refereed)
    Abstract [en]

    A novel artificial chaperone system using a combination of interactions between the unfolded protein, a detergent and a chromatographic column packed with immobilized β-cyclodextrin (β-CD) polymer coupled to an agarose gel, was introduced to refold recombinant Staphylococcus aureus elongation factor-G (EF-G). Pre-mixing of 10% Triton X-100 and unfolded EF-G at 24 mg/ml followed by a 20-fold dilution into refolding buffer led to successful capturing of EF-G by Triton X-100 resulting in formation of a detergent–protein complex at 1.2 mg/ml of final protein concentration. The complex was subsequently applied to the immobilized β-CD polymer column resulting in correct refolding of EF-G at a concentration of 530 μg/ml with 99% mass recovery. Detergent concentrations above critical micelle concentration were required for efficient capturing of EF-G at high protein concentration. Other detergents with hydrophile–lipophile-Balance values similar to that of Triton X-100 (Triton N-101, Noindet P40 (NP40), and Berol 185) also produced similar result. Soluble polymerized β-CD was more efficient than the monomer to remove the detergent from the protein complex in a batch system. Immobilized β-CD polymer column further improved the capability of detergent removal and was able to prevent aggregation that occurred with the addition of soluble β-CD polymer at high protein concentration in the batch system. The mechanism for this system-assisted refolding was tentatively interpreted: the released protein could correctly refold in an enclosed hydrophilic environment provided by the integration of matrix and β-CD polymer, and thus avoided aggregation during detergent removal.

  • 134. Li, Jing-Jing
    et al.
    Wang, Ai-Qing
    Janson, Jan-Christer
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry.
    Ballagi, Andras
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Chen, Jing
    Liu, Yong-Dong
    Ma, Guang-Hui
    Su, Zhi-Guo
    Immobilized Triton X-100-assisted refolding of Green Fluorescent Protein-Tobacco Etch Virus protease fusion protein using β-cyclodextrin as the eluent2009In: Process Biochemistry, ISSN 1359-5113, E-ISSN 1873-3298, Vol. 44, no 3, p. 277-282Article in journal (Refereed)
    Abstract [en]

    A new protein refolding technique based on the use of the non-charged detergent Triton X-100 immobilized to the cross-linked agarose gel Sepharose High Performance has been developed. The new solid phase was used in combination with soluble β-cyclodextrin (β-CD) to refold recombinant Green Fluorescent Protein fused to Tobacco Etch Virus protease (GFPTEVP) expressed as inclusion bodies in E. coli. Previous attempts to refold recombinant GFPTEVP by dilution had failed. In the new procedure a column packed with Triton X-100-coupled Sepharose High Performance was used to capture unfolded GFPTEVP followed by elution using an increasing β-CD concentration gradient. The yield of properly refolded GFPTEVP was 46% at a protein concentration of 380 μg/ml. In contrast, dilution refolding of GFPTEVP at 200 μg/ml refolding buffer resulted in only 4.7% of native protein.

  • 135.
    Lindberg, J. and Oscarsson, S
    Uppsala University, Centre for Surface Biotechnology.
    Surface Plasmon Resonance Technique for Studies of Protein Adsorption on Biomaterials1996In: 3: rd Meeting and Seminar on : Ceramics,Cells and Tissues, (Ed. Ravaglioli,A. and Krajewski,A.). Gruppo editoriale faenza editrice s.p.a., 1996, p. 171-178Conference paper (Other scientific)
  • 136.
    Linden, T., Ljunglöf, A., Kula, M-R. and Thömmes, J.
    Uppsala University, Centre for Surface Biotechnology.
    Visualizing two-component protein diffusion in porous adsorbents by confocal scanning laser microscopy1999In: Biotechnol. Bioeng., Vol. 65, no 2, p. 622-630Article in journal (Refereed)
  • 137.
    Lindholm, Johan
    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.
    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.
    Investigation of the adsorption behaviour of a chiral model compound on a tartardiamide-based network-polymeric chiral stationary phase2005In: Journal of Chromatography A, Vol. 1095, no 1-2, p. 50-59Article in journal (Refereed)
    Abstract [en]

    The adsorption behaviour of the enantiomers of 2-phenylbutyric acid on the chiral stationary phase (CSP) Kromasil CHI-TBB was studied using hexane/MTBE (90/10) as eluent. Adsorption isotherms were acquired at 40 different enantiomer concentrations in the interval between 7.6 μM and 305 mM, an approximately 40,000-fold dynamic range. The adsorption data fitted well to the bi-Langmuir model, indicating a heterogeneous surface with two different types of adsorption sites having different equilibrium constants and capacities; namely one chiral site and one non-chiral site. A comparison with earlier adsorption studies on modern CSPs revealed that the capacity value of the “true” chiral site of Kromasil CHI-TBB is the largest reported so far. The elution profiles simulated with these parameters show excellent agreement with the corresponding experimental profiles. Guidelines for comparisons of loading capacities of CSPs are presented.

  • 138.
    Lindholm, Johan
    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. Uppsala University, Disciplinary Domain of Science and Technology, Mathematics and Computer Science, Department of Information Technology, Numerical Analysis.
    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.
    Validation of the Accuracy of the Perturbation Peak Method for Determination of Multicomponent Adsorption Isotherm Parameters in LC2004In: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 76, p. 5472-5478Article in journal (Refereed)
  • 139.
    Lindholm, Johan
    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. Uppsala University, Disciplinary Domain of Science and Technology, Mathematics and Computer Science, Department of Information Technology, Numerical Analysis.
    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.
    Validation of the Accuracy of the Perturbation Peak Method for Determination of Single and Binary Adsorption Isotherm Parameters in LC2004In: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 76, p. 4856-4865Article in journal (Refereed)
  • 140.
    Ljunglöf, A. and Hjorth, R.
    Uppsala University, Centre for Surface Biotechnology.
    Confocal microscopy as a tool for studying protein adsorption to chromatographic matrices1996In: J. Chromatogr. A, Vol. 743, p. 75-83Article in journal (Refereed)
  • 141.
    Ljunglöf, A. and Thömmes, J.
    Uppsala University, Centre for Surface Biotechnology.
    Visualising intraparticle protein transport in porous adsorbents by confocal microscopy1998In: J. Chromatogr. A, Vol. 813, p. 387-395Article in journal (Refereed)
  • 142.
    Ljunglöf, A., Bergvall, P., Bhikhabhai, R. and Hjorth, R.
    Uppsala University, Centre for Surface Biotechnology.
    Direct visualization of plasmid DNA in individual chromatography adsorbent particles by confocal scanning laser microscopy1999In: J. Chromatogr. A, Vol. 844, p. 129-135Article in journal (Refereed)
  • 143.
    Lomniczi B., Wehmann E., Herczeg J., Ballagi-Pordany, A., Kaleta, E.F., Werner, O., Meulemans, G., Jorgensen, P.H., Mante, A.P., Gielkens, A.L., Capua, I., and Damoser, J.
    Uppsala University, Centre for Surface Biotechnology.
    Newcastle disease outbreaks in recent years in western Europe were caused by an old (VI) and a novel genotype (VII)1998In: Arch Virol, Vol. 143, no 1, p. 49-64Article in journal (Refereed)
  • 144. Luo, Jian
    et al.
    Leeman, Mats
    Ballagi, Andras
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Elfwing, Anders
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Su, Zhiguo
    Janson, Jan-Christer
    Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Surface Biotechnology. Department of Physical and Analytical Chemistry, Surface Biotechnology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical and Analytical Chemistry.
    Wahlund, Karl-Gustav
    Size characterization of green fluorescent protein inclusion bodies in E. coli using asymmetrical flow field-flow fractionation–multi-angle light scattering2006In: J. of Chromatography A, Vol. 1120, no 1-2, p. 158-164Article in journal (Refereed)
    Abstract [en]

    The goal of this study was to investigate the applicability of asymmetrical flow field-flow fractionation–multi-angle light scattering (AsFlFFF-MALS) for size analysis of green fluorescent protein inclusion bodies (GFPIBs). The size distributions of GFPIBs prepared by various culture conditions were determined. For GFPIBs prepared at 37 °C the peak maximum hydrodynamic diameter (dH) first increased and then decreased with the increase of the induction times in the presence of 0.1 and 2 mM isopropyl-β-d-thiogalactoside (IPTG). For GFPIBs prepared at 30 °C the peak maximum dH was constant at about 700 nm irrespectively of the induction times and IPTG concentrations.

  • 145.
    Luo, Q., Andrade, J.D. and Caldwell, K.D.
    Uppsala University, Centre for Surface Biotechnology.
    Thin Layer Ion-Exchange Chromatography of Proteins1998In: J. Chrom. A, Vol. 816, p. 97-105Article in journal (Refereed)
  • 146. Lv, Yong-Qin
    et al.
    Tan, Tian-Wei
    Wang, Man-Yi
    Janson, Jan-Christer
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    One-step rapid determination and purification of puerarin from Radix puerariae by n-octylamine-modified poly(methacrylate-co-ethylene dimethacrylate) monolith2008In: Journal of chromatography. B, ISSN 1570-0232, E-ISSN 1873-376X, Vol. 871, no 1, p. 1-6Article in journal (Refereed)
    Abstract [en]

    n-Octylamine-modified poly(methacrylate-co-ethylene dimethacrylate) monoliths were prepared for rapid screening, determination and one-step purification of puerarin from Radix puerariae (a crude extract of the root of Pueraria lobata). The modified monolith showed a specific surface area of 17.8 m(2) g(-1) an average pore size of 0.76 mu m and a total porosity of 60.8%. Fast separation of R. puerariae crude extract was achieved within 5 min at a flow velocity of 722 cm h(-1) resulting in a puerarin Purity of 97%, with a recovery of 85%. This demonstrates the potential of n-octylamine-modified poly(methacrylate-co-ethylene dimethacrylate) monolith for the rapid analysis and separation of isoflavonoids. Preparative scale sample loading (12 mg in 2 mL) resulted in a purity of 95%, and a recovery of about 69%. HPLC, FTIR, MS and H-1 NMR spectroscopy were used for the characterization and quantification of puerarin in isolated fraction.

  • 147.
    Lönnberg, Maria
    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.
    Lab-on-a-chip technology for determination of protein isoform profiles2006In: Journal of Chromatography A, ISSN 0021-9673, E-ISSN 1873-3778, Vol. 1127, no 1-2, p. 175-182Article in journal (Refereed)
    Abstract [en]

    A novel lab-on-a-chip technique for rapid (<15 min) and quantitative isoform-profile determination is presented. Ion-exchange chromatographic separation of protein-isoforms and a sensitive immunoassay detection are combined in a porous monolith chip. Thin lines of immobilized antibodies are used for specific capturing of target molecules, which can be detected by the reaction with antibodies bound to carbon black nano-strings. The bound carbon black is quantified by the use of an image scanner. As demonstrated with transferrin isoforms, differing only by 0.1 pH unit in their pI, this technology can distinguish minor differences in protein carbohydrate structure and enable specific determination of proteins in a complex environment, requiring only a few picogram of isoform for detection.

  • 148.
    Lönnberg, Maria
    et al.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Dehnes, Yvette
    Drevin, Malin
    Garle, Mats
    Lamon, Severine
    Leuenberger, Nicolas
    Quach, Trikien
    Carlsson, Jan
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Surface Biotechnology.
    Rapid affinity purification of erythropoietin from biological samples using disposable monoliths2010In: Journal of Chromatography A, ISSN 0021-9673, E-ISSN 1873-3778, Vol. 1217, no 45, p. 7031-7037Article in journal (Refereed)
    Abstract [en]

    Identification of post-translational modifications of proteins in biological samples often requires access to preanalytical purification and concentration methods In the purification step high or low molecular weight substances can be removed by size exclusion filters and high abundant proteins can be removed or low abundant proteins can be enriched by specific capturing tools In this paper is described the experience and results obtained with a recently emerged and easy-to-use affinity purification kit for enrichment of the low amounts of EPO found in urine and plasma specimens The kit can be used as a pre-step in the EPO doping control procedure as an alternative to the commonly used ultrafiltration for detecting aberrantly glycosylated isoforms The commercially available affinity purification kit contains small disposable anti-EPO monolith columns (6 mu L volume theta 7 mm length 0 15 mm) together with all required buffers A 24-channel vacuum manifold was used for simultaneous processing of samples The column concentrated EPO from 20 mL urine down to 55 mu L eluate with a concentration factor of 240 times while roughly 997% of non-relevant urine proteins were removed The recoveries of Neorecormon (epoetin beta) and the EPO analogues Aranesp and Mircera applied to buffer were high 76% 67% and 57% respectively The recovery of endogenous EPO from human urine was 65% High recoveries were also obtained when purifying human mouse and equine EPO from serum and human EPO from cerebrospinal fluid Evaluation with the accredited EPO doping control method based on isoelectric focusing (IEF) showed that the affinity purification procedure did not change the isoform distribution for rhEPO Aranesp Mircera or endogenous EPO The kit should be particularly useful for applications in which it is essential to avoid carry-over effects a problem commonly encountered with conventional particle-based affinity columns The encouraging results with EPO propose that similar affinity monoliths with the appropriate antibodies should constitute useful tools for general applications in sample preparation not only for doping control of EPO and other hormones such as growth hormone and insulin but also for the study of post-translational modifications of other low abundance proteins in biological and clinical research and for sample preparation prior to in vitro diagnostics.

  • 149.
    Malmsten, M., Xing, K. and Ljunglöf, A.
    Uppsala University, Centre for Surface Biotechnology.
    Confocal microscopy studies of trypsin immobilization on porous glycidyl methacrylate beads1999In: J. Colloid Interface Sci., Vol. 220, p. 436-442Article in journal (Refereed)
  • 150.
    Manta, C
    et al.
    Uppsala University, Centre for Surface Biotechnology.
    Ovsejevi, K
    Betancor, L
    Grazu, V
    Batistoni, J
    Batista-Viera, F
    Carlsson, J
    Introduction of thiol-reactive structures on to soluble and insoluble proteins2000In: BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY, ISSN 0885-4513, Vol. 31, p. 231-237Article in journal (Refereed)
    Abstract [en]

    When proteins containing disulphide groups were oxidized with magnesium monoperoxyphthalate at acidic pH, they acquired the property of binding thiol compounds. This was the case with the insoluble protein keratin, chosen for having a large number of disu

12345 101 - 150 of 234
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