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1.
  • Asplund, Maria, 1978-, et al. (författare)
  • Composite biomolecule/PEDOT materials for neural electrodes
  • 2008
  • Ingår i: Biointerphases. - NY : American Institute of Physics. - 1559-4106. ; 3:3, s. 83-93
  • Tidskriftsartikel (refereegranskat)abstract
    • Electrodes intended for neural communication must be designed to meet boththe electrochemical and biological requirements essential for long term functionality. Metallic electrode materials have been found inadequate to meet theserequirements and therefore conducting polymers for neural electrodes have emergedas a field of interest. One clear advantage with polymerelectrodes is the possibility to tailor the material to haveoptimal biomechanical and chemical properties for certain applications. To identifyand evaluate new materials for neural communication electrodes, three chargedbiomolecules, fibrinogen, hyaluronic acid (HA), and heparin are used ascounterions in the electrochemical polymerization of poly(3,4-ethylenedioxythiophene) (PEDOT). The resultingmaterial is evaluated electrochemically and the amount of exposed biomoleculeon the surface is quantified. PEDOT:biomolecule surfaces are also studiedwith static contact angle measurements as well as scanning electronmicroscopy and compared to surfaces of PEDOT electrochemically deposited withsurfactant counterion polystyrene sulphonate (PSS). Electrochemical measurements show that PEDOT:heparinand PEDOT:HA, both have the electrochemical properties required for neuralelectrodes, and PEDOT:heparin also compares well to PEDOT:PSS. PEDOT:fibrinogen isfound less suitable as neural electrode material.
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2.
  • Cicortas Gunnarsson, Lavinia, et al. (författare)
  • A carbohydrate binding module as a diversity-carrying scaffold
  • 2004
  • Ingår i: Protein Engineering Design & Selection. - : Oxford University Press. - 1741-0126 .- 1741-0134. ; 17:3, s. 213-221
  • Tidskriftsartikel (refereegranskat)abstract
    • The growing field of biotechnology is in constant need of binding proteins with novel properties. Not just binding specificities and affinities but also structural stability and productivity are important characteristics for the purpose of large-scale applications. In order to find such molecules, libraries are created by diversifying naturally occurring binding proteins, which in those cases serve as scaffolds. In this study, we investigated the use of a thermostable carbohydrate binding module, CBM4-2, from a xylanase found in Rhodothermus marinus, as a diversity-carrying scaffold. A combinatorial library was created by introducing restricted variation at 12 positions in the carbohydrate binding site of the CBM4-2. Despite the small size of the library (1.6x10(6) clones), variants specific towards different carbohydrate polymers (birchwood xylan, Avicel and ivory nut mannan) as well as a glycoprotein (human IgG4) were successfully selected for, using the phage display method. Investigated clones showed a high productivity (on average 69 mg of purified protein/l shake flask culture) when produced in Escherichia coli and they were all stable molecules displaying a high melting transition temperature (75.7 +/- 5.3degreesC). All our results demonstrate that the CBM4-2 molecule is a suitable scaffold for creating variants useful in different biotechnological applications.
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3.
  • de Maré, L, et al. (författare)
  • A cultivation technique for E. coli fed-batch cultivations operating close to the maximum oxygen transfer capacity of the reactor
  • 2005
  • Ingår i: Biotechnology Letters. - : Springer. - 0141-5492 .- 1573-6776. ; 27:14, s. 983-990
  • Tidskriftsartikel (refereegranskat)abstract
    • A cultivation strategy combining the advantages of temperature-limited fed-batch and probing feeding control is presented. The technique was evaluated in fed-batch cultivations with E. coli BL21(DE3) producing xylanase in a 3 liter bioreactor. A 20% increase in cell mass was achieved and the usual decrease in specific enzyme activity normally observed during the late production phase was diminished with the new technique. The method was further tested by growing E. coli W3110 in a larger bioreactor (50 l). It is a suitable cultivation technique when the O2 transfer capacity of the reactor is reached and it is desired to continue to produce the recombinant protein.
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4.
  • Jujic, Amra, et al. (författare)
  • Glucose-dependent insulinotropic peptide and risk of cardiovascular events and mortality : a prospective study
  • 2020
  • Ingår i: Diabetologia. - : Springer. - 0012-186X .- 1432-0428. ; 63:5, s. 1043-1054
  • Tidskriftsartikel (refereegranskat)abstract
    • Aims/hypothesis: Evidence that glucose-dependent insulinotropic peptide (GIP) and/or the GIP receptor (GIPR) are involved in cardiovascular biology is emerging. We hypothesised that GIP has untoward effects on cardiovascular biology, in contrast to glucagon-like peptide 1 (GLP-1), and therefore investigated the effects of GIP and GLP-1 concentrations on cardiovascular disease (CVD) and mortality risk.Methods: GIP concentrations were successfully measured during OGTTs in two independent populations (Malmo Diet Cancer-Cardiovascular Cohort [MDC-CC] and Prevalence, Prediction and Prevention of Diabetes in Botnia [PPP-Botnia]) in a total of 8044 subjects. GLP-1 (n = 3625) was measured in MDC-CC. The incidence of CVD and mortality was assessed via national/regional registers or questionnaires. Further, a two-sample Mendelian randomisation (2SMR) analysis between the GIP pathway and outcomes (coronary artery disease [CAD] and myocardial infarction) was carried out using a GIP-associated genetic variant, rs1800437, as instrumental variable. An additional reverse 2SMR was performed with CAD as exposure variable and GIP as outcome variable, with the instrumental variables constructed from 114 known genetic risk variants for CAD.Results: In meta-analyses, higher fasting levels of GIP were associated with risk of higher total mortality (HR[95% CI] = 1.22 [1.11, 1.35]; p = 4.5 x 10(-5)) and death from CVD (HR[95% CI] 1.30 [1.11, 1.52]; p = 0.001). In accordance, 2SMR analysis revealed that increasing GIP concentrations were associated with CAD and myocardial infarction, and an additional reverse 2SMR revealed no significant effect of CAD on GIP levels, thus confirming a possible effect solely of GIP on CAD.Conclusions/interpretation: In two prospective, community-based studies, elevated levels of GIP were associated with greater risk of all-cause and cardiovascular mortality within 5-9 years of follow-up, whereas GLP-1 levels were not associated with excess risk. Further studies are warranted to determine the cardiovascular effects of GIP per se.
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5.
  • Mårtensson, Olof, et al. (författare)
  • Effects of fermented, ropy, non-dairy, oat-based products on serum lipids and the faecal excretion of cholesterol and short chain fatty acids in germfree and conventional rats
  • 2002
  • Ingår i: Nutrition Research. - : Elsevier. - 0271-5317. ; 22:12, s. 1461-1473
  • Tidskriftsartikel (refereegranskat)abstract
    • Three fermented, ropy, non-dairy, oat-based products were evaluated for their effect on serum lipids, faecal cholesterol and faecal short chain fatty. acids in germfree and conventional rats. Three different exopolysaccharide (EPS) producing lactic acid bacteria strains were used to ferment the non-dairy oat-base (Adavena(R) G40) (Ceba Foods AB, Lund; Sweden). Two commercial non-dairy products based on oats (Mill Milk(TM)) (Ceba Foods AB, Lund, Sweden) and rice (Rice Dream(R)) (Imagine Foods, London, UK) were used as non-ropy and unfermented controls. All the standardized feeds were sterilized before being fed to the animals. Adult, germfree-and conventional AGUS rats, were fed the above sterile diets ad libitum for 21 days. Blood samples and faecal samples were collected and the animals' weight gain was monitored throughout the study. No significant change in serum lipids or faecal excretion of cholesterol was observed between the groups on the different diets. A difference in faecal SCFA pattern was observed in conventional rats fed on the oat-based diets in comparison. to the group fed on the rice-based diet. More evidence is needed to support the effect of fermented, ropy, oat-based products and their potential effect on serum lipids, faecal cholesterol/coprostanol levels and amounts of short chain fatty acids.
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6.
  • Mårtensson, Olof, et al. (författare)
  • Fermented, ropy, oat-based products reduce cholesterol levels and stimulate the bifidobacteria flora in humans
  • 2005
  • Ingår i: Nutrition Research. - : Elsevier. - 0271-5317. ; 25:5, s. 429-442
  • Tidskriftsartikel (refereegranskat)abstract
    • This investigation determined the effects of fermented oat-based products containing both native and microbial beta-glucans on plasma lipids and on fecal total bacterial count and Bifidobacterium ssp. The study was randomized, double blind with 3 parallel groups. Sixty-two free-living volunteers with moderately increased plasma cholesterol levels were recruited. In the final analysis, 56 subjects remained, as 6 subjects had left the study either due to lack of time (n = 2), unwillingness to continue the regimen (n = 2), or for other reasons (n = 2). During the first 3 weeks, all subjects received a fermented dairy-based product (control product, run-in period). On the following 5 weeks, I group continued with the control product, whereas the other 2 groups were given fermented oat-based products (intervention period, 3-3.5 g native beta-glucans per day). One of the oat products (ropy) was cofermented with an exopolysaccharide-producing strain, Pediococcus damnosus 2.6. A significant (P = .022) reduction in total cholesterol by 6% was observed in volunteers who had eaten the fermented, ropy, oat-based product compared with the control group. No other significant changes in plasma lipids were found. A significant increase in total bacterial count (P = .001) and Bifidobacterium ssp (P = .012) was observed in fecal samples from volunteers in the group who had eaten the fermented, ropy, oat-based product. This study shows that a fermented, ropy, oat-based product, containing both native and microbial glucans, can reduce the blood cholesterol level and also stimulate the bifidobacteria flora in the gastrointestinal tract. (c) 2005 Elsevier Inc. All rights reserved.
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7.
  • Thaning, Elin M., et al. (författare)
  • Stability of Poly(3,4-ethylene dioxythiophene) Materials Intended for Implants
  • 2010
  • Ingår i: Journal of Biomedical Materials Research - Part B Applied Biomaterials. - : John Wiley and Sons, Ltd. - 1552-4973. ; 93B93:2, s. 407-415
  • Tidskriftsartikel (refereegranskat)abstract
    • This study presents experiments designed to study the stability of the conducting polymer poly(3,4-ethylene dioxythiophene) (PEDOT), under simulated physiological conditions using phosphate-buffered saline (PBS) and hydrogen peroxide (H2O2) (0 01M) at 37 degrees C over a 5- to 6-week period Voltage pulsing in PBS was used as an additional test environment The influence of switching the counter ion used in electropolymerization from polystyrene sulphonate (PSS) to heparin was investigated Absorbance spectroscopy and cyclic voltammetry were used to evaluate the material properties Most of the samples in H2O2 lost both electroactivity and optical absorbance within the study period, but PEDOT.PSS was found slightly more stable than PEDOT heparin. Polymers were relatively stable in PBS throughout the study period, with around 80% of electroactivity remaining after 5 weeks, disregarding delamination, which was a significant problem especially for polymer on indium tin oxide substrates Voltage pulsing in PBS did not increase degradation. The counter ion influenced the time course of degradation in Oxidizing agents.
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8.
  • Abou-Hachem, Maher, et al. (författare)
  • Calcium binding and thermostability of carbohydrate binding module CBM4-2 of Xyn10A from Rhodothermus marinus.
  • 2002
  • Ingår i: Biochemistry. - : The American Chemical Society (ACS). - 0006-2960. ; 41:18, s. 5720-5729
  • Tidskriftsartikel (refereegranskat)abstract
    • Calcium binding to carbohydrate binding module CBM4-2 of xylanase 10A (Xyn10A) from Rhodothermus marinus was explored using calorimetry, NMR, fluorescence, and absorbance spectroscopy. CBM4-2 binds two calcium ions, one with moderate affinity and one with extremely high affinity. The moderate-affinity site has an association constant of (1.3 +/- 0.3) x 10(5) M(-1) and a binding enthalpy DeltaH(a) of -9.3 +/- 0.4 kJ x mol(-1), while the high-affinity site has an association constant of approximately 10(10) M(-1) and a binding enthalpy DeltaH(a) of -40.5 +/- 0.5 kJ x mol(-1). The locations of the binding sites have been identified by NMR and structural homology, and were verified by site-directed mutagenesis. The high-affinity site consists of the side chains of E11 and D160 and backbone carbonyls of E52 and K55, while the moderate-affinity site comprises the side chain of D29 and backbone carbonyls of L21, A22, V25, and W28. The high-affinity site is in a position analogous to the calcium site in CBM4 structures and in a recent CBM22 structure. Binding of calcium increases the unfolding temperature of the protein (T(m)) by approximately 23 degrees C at pH 7.5. No correlation between binding affinity and T(m) change was noted, as each of the two calcium ions contributes almost equally to the increase in unfolding temperature.
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9.
  • Abou Hachem, Maher, et al. (författare)
  • Carbohydrate-binding modules from a thermostable Rhodothermus marinus xylanase : Cloning, expression and binding studies
  • 2000
  • Ingår i: Biochemical Journal. - : Portland Press. - 0264-6021. ; 345:1, s. 53-60
  • Tidskriftsartikel (refereegranskat)abstract
    • The two N-terminally repeated carbohydrate-binding modules (CBM4-1 and CBM4-2) encoded by xyn10A from Rhodothermus marinus were produced in Escherichia coli and purified by affinity chromatography. Binding assays to insoluble polysaccharides showed binding to insoluble xylan and to phosphoric-acid-swollen cellulose but not to Avicel or crystalline cellulose. Binding to insoluble substrates was significantly enhanced by the presence of Na+ and Ca2+ ions. The binding affinities for soluble polysaccharides were tested by affinity electrophoresis; strong binding occurred with different xylans and β-glucan. CBM4-2 displayed a somewhat higher binding affinity than CBM4-1 for both soluble and insoluble substrates but both had similar specificities. Binding to short oligosaccharides was measured by NMR; both modules bound with similar affinities. The binding of the modules was shown to be dominated by enthalpic forces. The binding modules did not contribute with any significant synergistic effects on xylan hydrolysis when incubated with a Xyn10A catalytic module. This is the first report of family 4 CBMs with affinity for both insoluble xylan and amorphous cellulose.
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10.
  • Abou-Hachem, Maher, et al. (författare)
  • The modular organisation and stability of a thermostable family 10 xylanase
  • 2003
  • Ingår i: Biocatalysis and Biotransformation. - : Taylor & Francis. - 1024-2422. ; 21:5-6, s. 253-260
  • Tidskriftsartikel (refereegranskat)abstract
    • The thermophilic marine bacterium Rhodothermus marinus produces a modular family 10 xylanase (Xyn10A). It consists of two N-terminal family 4 carbohydrate binding modules (CBMs) followed by a domain of unknown function (D3), and a catalytic module (CM) flanked by a small fifth domain (D5) at its C-terminus. Several truncated mutants of the enzyme have been produced and characterised with respect to biochemical properties and stability. Multiple calcium binding sites are shown to be present in the two N-terminal CBMs and recent evidence suggests that the third domain of the enzyme also has the ability to bind the same metal ligand. The specific binding of Ca2+ was demonstrated to have a pronounced effect on thermostability as shown by differential scanning calorimetry and thermal inactivation studies. Furthermore, deletion mutants of the enzyme were less stable than the full-length enzyme suggesting that module interactions contributed to the stability of the enzyme. Finally, recent evidence indicates that the fifth domain of Xyn10A is a novel type of module mediating cell-attachment.
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