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Sökning: WFRF:(Ersson Bo)

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1.
  • Xue, Bo, et al. (författare)
  • Chromatographic and fluorometric study of interactions between thiophilic and hydrophobic ligands and tryptophan peptide homologues
  • 2006
  • Ingår i: Journal of Chromatography A. ; 1107:1-2, s. 46-51
  • Tidskriftsartikel (refereegranskat)abstract
    • The interactions of tryptophan and its peptide homologues with thiophilic ligands were studied in terms of their chromatographic retention and steady-state fluorescence under various conditions, and compared with non-polar structures typically regarded as pure hydrophobic ligands. The experimental results show that both non-polar and polar interactions are involved in what has been termed “thiophilic adsorption chromatography”.
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2.
  • Arnell, Robert, et al. (författare)
  • Biotechnological Approach to the Synthesis of 9α-Hydroxylated Steroids
  • 2007
  • Ingår i: Preparative Biochemistry & Biotechnology. - : Informa UK Limited. - 1082-6068 .- 1532-2297. ; 37:4, s. 309-321
  • Tidskriftsartikel (refereegranskat)abstract
    • The steroid 9α-hydroxylase gene has been cloned from Mycobacterium smegmatis into Escherichia coli BL21. Progesterone added to bioreactors was subjected to in vivo transformation into 9α-hydroxyprogesterone. In 7 days, 43.6 mg9α-hydroxyprogesterone was formed from 53.8 mg/L progesterone. The enzyme also has shown evidence of processing 4-androstene-3,17-dione in vivo. An extensive analytical method development, including LLE, HPLC-DAD, MS, andNMR was performed to verify the product and to enable a quantitative analysis. Protocols for analytical and preparative separation have been developed, using binaphtol as internal standard. Both the growth pattern and the bioconversion ratewere unaffected by the presence of binaphtol in the bioreactor. The enzyme was purified by immobilised metal affinity and ion exchange chromatography, resulting in low in vitro activity.
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4.
  • Gottschalk, Ingo, et al. (författare)
  • Improved lectin-mediated immobilization of human red blood cells in superporous agarose beads
  • 2003
  • Ingår i: Journal of chromatography. B. - 1570-0232 .- 1873-376X. ; 784:1, s. 203-208
  • Tidskriftsartikel (refereegranskat)abstract
    • A new type of agarose bead, superporous agarose, was used as a gel support for immobilization of human red blood cells (RBCs) mediated by wheat germ lectin. The number of immobilized cells was similar to that obtained with commercial wheat germ lectin–agarose but the cell stability appeared to be superior. This allowed improved frontal affinity chromatographic analyses of cytochalasin B (CB)-binding to the glucose transporter GLUT1 which established a ratio of one CB-binding site per GLUT1 dimer for both plain RBCs or those treated with different poly amino acids. The measured dissociation constants, 70±14 nM for CB and 12±3 mM for glucose binding to GLUT1, are similar to those reported earlier.
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  • Resultat 1-5 av 5
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refereegranskat (3)
övrigt vetenskapligt/konstnärligt (1)
populärvet., debatt m.m. (1)
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Ersson, Bo (4)
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