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Träfflista för sökning "WFRF:(Janson Christer) ;hsvcat:1"

Sökning: WFRF:(Janson Christer) > Naturvetenskap

  • Resultat 1-10 av 36
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1.
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2.
  • Hao, Dong-Xia, et al. (författare)
  • Residue-level elucidation of the ligand-induced protein binding on phenyl-argarose microspheres by NMR hydrogen/deuterium exchange technique
  • 2012
  • Ingår i: Soft Matter. - : Royal Society of Chemistry (RSC). - 1744-683X .- 1744-6848. ; 8:23, s. 6248-6255
  • Tidskriftsartikel (refereegranskat)abstract
    • Protein-ligand interactions on liquid-solid interfaces governed the design of functional biomaterials. However, accurate residue details of ligand induced protein binding and unfolding on an interface were still unknown by the current ensemble of protein structure characterizations. Here, a hydrogen/deuterium (H/D) approach coupled with analysis of NMR TOCSY spectra and the solvent accessible surface area (SASA) was designed to enable residue level understanding of lysozyme adsorbed at a phenyl-ligand modified surface. Results showed that the binding sites and unfolding of lysozyme molecules on phenyl-agarose microspheres demonstrated significant ligand-density dependence and protein-coverage dependence. Either increasing ligand density or decreasing adsorption coverage would lead to more binding sites and unfolding of the protein molecules. With the multipoint adsorption strengthening, the protein molecule changed from lying end-on to side-on. Finally, Molecular Dock simulation was utilized to evaluate the NMR determined binding sites based on energy ranking of the binding. It confirmed that this NMR approach represents a reliable route to in silico abundant residue-level structural information during protein interaction with biomaterials.
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3.
  • Batista-Viera, F, et al. (författare)
  • Affinity chromatography
  • 2011. - 3
  • Ingår i: Protein Purification, Principles, High Resolution Methods and Applications. - : John Wiley & Sons Inc.. - 9780471746614 ; , s. 221-258
  • Bokkapitel (övrigt vetenskapligt/konstnärligt)
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4.
  • Ersson, B, et al. (författare)
  • Introduction to protein purification
  • 2011. - 3
  • Ingår i: Protein Purification, Principles, High Resolution Methods and Applications. - : John Wiley & Sons Inc.. - 9780471746614 ; , s. 3-22
  • Bokkapitel (övrigt vetenskapligt/konstnärligt)
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5.
  • Gao, Min, et al. (författare)
  • Separation of polyphenols using porous polyamide resin and assessment of mechanism of retention
  • 2011
  • Ingår i: Journal of Separation Science. - : Wiley. - 1615-9306 .- 1615-9314. ; 34:15, s. 1853-1858
  • Tidskriftsartikel (refereegranskat)abstract
    • A porous polyamide resin is shown to possess hydrogen bond acceptor properties suitable for the separation of polyphenolic solutes such as phenolic acids, flavonols and flavonoids. The separation is achieved in the presence of solvent mixtures of acetic acid and ethanol. The extent of hydrogen bond adsorption is reviewed based on data obtained from the elution behaviour of a variety of simple polyphenolic solutes. Polyamide adsorption chromatography was applied for the purification of resveratrol and polydatin from Polygonum cuspidatum Sieb. & Zucc.
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6.
  • Janson, Jan-Christer, et al. (författare)
  • Introduction to chromatography
  • 2011. - 3
  • Ingår i: Protein Purification, Principles, High Resolution Methods and Applications. - : John Wiley & Sons Inc.. - 9780471746614 ; , s. 25-50
  • Bokkapitel (övrigt vetenskapligt/konstnärligt)
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7.
  • Larsson, Anna M., et al. (författare)
  • Three-dimensional crystal structure and enzymic characterization of beta-mannanase Man5A from blue mussel Mytilus edulis
  • 2006
  • Ingår i: Journal of Molecular Biology. - : Elsevier BV. - 1089-8638 .- 0022-2836. ; 357:5, s. 1500-1510
  • Tidskriftsartikel (refereegranskat)abstract
    • 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 1.6 angstrom 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 (beta alpha)(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. (c) 2006 Elsevier Ltd. All rights reserved.
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8.
  • Li, Jing-Jing, et al. (författare)
  • Immobilized Triton X-100-assisted refolding of Green Fluorescent Protein-Tobacco Etch Virus protease fusion protein using β-cyclodextrin as the eluent
  • 2009
  • Ingår i: Process Biochemistry. - : Elsevier BV. - 1359-5113 .- 1873-3298. ; 44:3, s. 277-282
  • Tidskriftsartikel (refereegranskat)abstract
    • 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.
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9.
  • Liu, Dan, et al. (författare)
  • Liquid-liquid/solid three-phase high-speed counter-current chromatography, a new technique for separation of polyphenols from Geranium wilfordii Maxim
  • 2012
  • Ingår i: Journal of Separation Science. - : Wiley. - 1615-9306 .- 1615-9314. ; 35:16, s. 2146-2151
  • Tidskriftsartikel (refereegranskat)abstract
    • High-speed counter-current chromatography using a new liquidliquid/solid three-phase system was used for the separation of the polyphenols corilagin and geraniin from a crude extract of Geranium wilfordii Maxim in one step. The optimized three-phase system was composed of n-hexane/ethyl acetate/methanol/acetic acid/water and to which was added 10-mu m average diameter microspheres of cross-linked 12% agarose at the ratio of 0.2:10:2:1:5 and 0.1 g/mL, respectively. The purities of geraniin and corilagin were 82 and 90%, which were determined by HPLC at 280 nm. A 14.5 and 7 mg of geraniin and corilagin were purified from 160 mg crude extract with the yields of 70 and 78%, respectively.
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10.
  • Liu, Dan, et al. (författare)
  • One-step separation and purification of hydrolysable tannins from Geranium wilfordii Maxim by adsorption chromatography on cross-linked 12% agarose gel
  • 2011
  • Ingår i: Journal of Separation Science. - : Wiley. - 1615-9306 .- 1615-9314. ; 34:9, s. 995-998
  • Tidskriftsartikel (refereegranskat)abstract
    • The hydrolysable tannins corilagin and geraniin, the major active components of the traditional Chinese medicine Geranium wilfordii Maxim, have been separated and purified from crude extracts in one step by adsorption chromatography on cross-linked 12% agarose gel (Superose 12 10/300 GL). The separation was achieved by gradient elution using mobile phase A composed of 5% ethanol and 5% acetic acid and mobile phase B composed of 30% ethanol and 30% acetic acid. The gradients were composed as follows: 0-240 mL, 0-25% B; 240-480 mL, 25-40% B; after 480 mL, 100% B. The purities of the collected corilagin and geraniin were 92.4 and 87.2%, and the corresponding yields were 88.0 and 76.8%, respectively.
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  • Resultat 1-10 av 36

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