https://www.mdu.se/

mdu.sePublications
Change search
Refine search result
1 - 8 of 8
CiteExportLink to result list
Permanent link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Rows per page
  • 5
  • 10
  • 20
  • 50
  • 100
  • 250
Sort
  • Standard (Relevance)
  • Author A-Ö
  • Author Ö-A
  • Title A-Ö
  • Title Ö-A
  • Publication type A-Ö
  • Publication type Ö-A
  • Issued (Oldest first)
  • Issued (Newest first)
  • Created (Oldest first)
  • Created (Newest first)
  • Last updated (Oldest first)
  • Last updated (Newest first)
  • Disputation date (earliest first)
  • Disputation date (latest first)
  • Standard (Relevance)
  • Author A-Ö
  • Author Ö-A
  • Title A-Ö
  • Title Ö-A
  • Publication type A-Ö
  • Publication type Ö-A
  • Issued (Oldest first)
  • Issued (Newest first)
  • Created (Oldest first)
  • Created (Newest first)
  • Last updated (Oldest first)
  • Last updated (Newest first)
  • Disputation date (earliest first)
  • Disputation date (latest first)
Select
The maximal number of hits you can export is 250. When you want to export more records please use the Create feeds function.
  • 1.
    Buijs, Jos
    et al.
    Mälardalen University, Department of Biology and Chemical Engineering.
    Håkansson, Kristina
    Uppsala University, Sweden.
    Hagman, Charlotte
    Uppsala University, Sweden.
    Håkansson, Per
    Uppsala University, Sweden.
    Oscarsson, Sven
    Mälardalen University, Department of Biology and Chemical Engineering.
    A new method for the accurate determination of the isotopic state of single amide hydrogens within peptides using Fourier transform ion cyclotron resonance mass spectrometry2000In: Rapid Communications in Mass Spectrometry, ISSN 0951-4198, Vol. 14, no 19, p. 1751-1756Article in journal (Refereed)
    Abstract [en]

    A new method is presented to accurately determine the probability of having a deuterium or hydrogen atom on a specific amide position within a peptide after deuterium/hydrogen (D/H) exchange in solution. Amide hydrogen exchange has been proven to be a sensitive probe for studying protein structures and structural dynamics. At the same time, mass spectrometry in combination with physical fragmentation methods is commonly used to sequence proteins based on an amino acid residue specific mass analysis. In the present study it is demonstrated that the isotopic patterns of a series of peptide fragment ions obtained with capillary-skimmer dissociation, as observed with a 9.4 T Fourier transform ion cyclotron resonance (FTICR) mass spectrometer, can be used to calculate the isotopic state of specific amide hydrogens. This calculation is based on the experimentally observed isotopic patterns of two consecutive fragments and on the isotopic binomial distributions of the atoms in the residue constituting the difference between these two consecutive fragments. The applicability of the method is demonstrated by following the sequence-specific D/H exchange rate in solution of single amide hydrogens within some peptides.

  • 2.
    Karlsson, Anders
    et al.
    Gothenburg University, Sweden.
    Karlsson, Roger
    Gothenburg University, Sweden.
    Karlsson, Mattias
    Gothenburg University, Sweden.
    Cans, Annsofie
    Gothenburg University, Sweden.
    Strömberg, Anette
    Gothenburg University, Sweden.
    Ryttsén, Frida
    Gothenburg University, Sweden.
    Orwar, Owe
    Chalmers University of Technology, Sweden.
    Molecular engineering: Networks of nanotubes and containers2001In: Nature, ISSN 0028-0836, E-ISSN 1476-4687, Vol. 409, no 6817, p. 150-152Article in journal (Refereed)
  • 3.
    Olofsson, Jessica
    et al.
    Chalmers University of Technology, Gothenburg, Sweden .
    Levin, Mikael
    Cellectricon AB, Gothenburg, Sweden.
    Strömberg, Anette
    Cellectricon AB, Gothenburg, Sweden.
    Weber, Stephen
    University of Pittsburgh, United States.
    Ryttsén, Frida
    Cellectricon AB, Gothenburg, Sweden.
    Orwar, Owe
    Chalmers University of Technology, Gothenburg, Sweden .
    Scanning electroporation of selected areas of adherent cell cultures2007In: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 79, no 12, p. 4410-4418Article in journal (Refereed)
    Abstract [en]

    We present a computer-controlled scanning electroporation method. Adherent cells are electroporated using an electrolyte-filled capillary in contact with an electrode. The capillary can be scanned over a cell culture and locally deliver both an electric field and an electroporation agent to the target area without affecting surrounding cells. The instantaneous size of the targeted area is determined by the dimensions of the capillary. The size and shape of the total electroporated area are defined by these dimensions in combination with the scanning pattern. For example, striped and serpentine patterns of electroporated cells in confluent cultures can be formed. As it is easy to switch between different electroporation agents, the method is suitable for design of cell cultures with complex composition. Finite element method simulations were used to study the spatial distributions of the electric field and the concentration of an electroporation agent, as well as the fluid dynamics related to scanning and flow ofelectroporation agent from the capillary. The method was validated for transfection by introduction of a 9-base-pair-long randomized oligonucleotide into PC12 cells and a pmaxGFP plasmid coding for green fluorescent protein into CHO and WSS cells.

  • 4.
    Oscarsson, Sven
    et al.
    Mälardalen University, Department of Biology and Chemical Engineering.
    Kårsnäs, Per
    PerCreative, Gothenburg, Sweden.
    Salt-promoted adsorption of proteins onto amphiphilic agarose-based adsorbents. II. Effects of salt and salt concentration1998In: Journal of Chromatography A, ISSN 0021-9673, Vol. 803, no 1-2, p. 83-93Article in journal (Refereed)
    Abstract [en]

    The effects of different types of salts and salt concentrations on the selectivity in the adsorption of serum proteins have been compared for the amphiphilic agarose-based adsorbents Phenyl-Sepharose, Octyl-Sepharose, butyl-agarose and mercaptopyridine-derivatized agarose. By use of multivariate analysis, the complex interrelationships for the different combined effects were evaluated. From these analyses conclusions about similarities and/or dissimilarities in the mechanisms involved in adsorption of proteins on respective adsorbent were made.

  • 5.
    Skvaril, Jan
    et al.
    Mälardalen University, School of Business, Society and Engineering, Future Energy Center.
    Kyprianidis, Konstantinos
    Mälardalen University, School of Business, Society and Engineering, Future Energy Center.
    Avelin, Anders
    Mälardalen University, School of Business, Society and Engineering, Future Energy Center.
    Odlare, Monica
    Mälardalen University, School of Business, Society and Engineering, Future Energy Center.
    Dahlquist, Erik
    Mälardalen University, School of Business, Society and Engineering, Future Energy Center.
    Fast Determination of Fuel Properties in Solid Biofuel Mixtures by Near Infrared Spectroscopy2017In: Energy Procedia, ISSN 1876-6102, Vol. 105, p. 1309-1317Article in journal (Refereed)
    Abstract [en]

    This paper focuses on the characterization of highly variable biofuel properties such as moisture content, ash content and higher heating value by near-infrared (NIR) spectroscopy. Experiments were performed on different biofuel sample mixtures consisting of stem wood chips, forest residue chips, bark, sawdust, and peat. NIR scans were performed using a Fourier transform NIR instrument, and reference values were obtained according to standardized laboratory methods. Spectral data were pre-processed by Multiplicative scatter correction correcting light scattering and change in a path length for each sample. Multivariate calibration was carried out employing Partial least squares regression while absorbance values from full NIR spectral range (12,000–4000 cm-1), and reference values were used as inputs. It was demonstrated that different solid biofuel properties can be measured by means of NIR spectroscopy. The accuracy of the models is satisfactory for industrial implementation towards improved process control. 

  • 6.
    Skvaril, Jan
    et al.
    Mälardalen University, School of Business, Society and Engineering, Future Energy Center.
    Kyprianidis, Konstantinos
    Mälardalen University, School of Business, Society and Engineering, Future Energy Center.
    Dahlquist, Erik
    Mälardalen University, School of Business, Society and Engineering, Future Energy Center.
    Applications of near-infrared spectroscopy (NIRS) in biomass energy conversion processes: A review2017In: Applied spectroscopy reviews (Softcover ed.), ISSN 0570-4928, E-ISSN 1520-569X, Vol. 52, no 8, p. 675-728Article, review/survey (Refereed)
    Abstract [en]

    Biomass used in energy conversion processes is typically characterized by high variability, making its utilization challenging. Therefore, there is a need for a fast and non-destructive method to determine feedstock/product properties and directly monitor process reactors. The near-infrared spectroscopy (NIRS) technique together with advanced data analysis methods offers a possible solution. This review focuses on the introduction of the NIRS method and its recent applications to physical, thermochemical, biochemical and physiochemical biomass conversion processes represented mainly by pelleting, combustion, gasification, pyrolysis, as well as biogas, bioethanol, and biodiesel production. NIRS has been proven to be a reliable and inexpensive method with a great potential for use in process optimization, advanced control, or product quality assurance.

  • 7.
    Strömberg, Anette
    University of Gothenburg.
    Manipulating and Mimicking Single-Cell Compartments Using Liposome Chemistry and Miniaturized Biomembrane Electropermeabilization2001Doctoral thesis, comprehensive summary (Other academic)
  • 8.
    Östlund, Lena
    Mälardalen University, School of Sustainable Development of Society and Technology.
    Development of a Multiresidue Method for Analysis of Acidic Pesticides in Cereals with Liquid Chromatography-Tandem Mass Spectrometry2009Independent thesis Advanced level (degree of Master (One Year)), 20 credits / 30 HE creditsStudent thesis
    Abstract [en]

    A new method for analysis of acidic herbicides, mostly phenoxy acids and their esters, in cereals with liquid chromatography-tandem quadrupole mass spectrometry (LS-MS/MS) has been developed. Samples were hydrolyzed with sodium hydroxide in order to release covalently bound compounds followed by neutralization and finally extraction with acidified ethyl acetate. The extraction efficiency for both ester formulations and acids were studied. Acceptable results (70-120 %) were obtained for 2,4-D, dichlorprop, MCPA and mecoprop for both esters and acids. However, low recoveries were observed for ester formulations of dicamba, fluroxypyr, fluazifop and haloxyfop, possibly due to the complex structure of the compounds in combination with the matrix and/or incomplete hydrolysis step. The limit of quantification (LOQ) for targeted pesticides was 0.01 mg/kg. The method has been tested in the EU Proficiency Test for cereals with good results.

    Download full text (pdf)
    FULLTEXT01
1 - 8 of 8
CiteExportLink to result list
Permanent link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf