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Träfflista för sökning "WFRF:(Jornvall H.) srt2:(2000-2004)"

Sökning: WFRF:(Jornvall H.) > (2000-2004)

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  • Johansson, K, et al. (författare)
  • Crystal structure of sorbitol dehydrogenase
  • 2001
  • Ingår i: Chemico-biological interactions. - : Elsevier BV. - 0009-2797. ; 130130-132:1-3, s. 351-358
  • Tidskriftsartikel (refereegranskat)
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  • Norberg, A, et al. (författare)
  • Identification of the bioactive peptide PEC-60 in brain
  • 2003
  • Ingår i: Cellular and molecular life sciences : CMLS. - : Springer Science and Business Media LLC. - 1420-682X .- 1420-9071. ; 60:2, s. 378-381
  • Tidskriftsartikel (refereegranskat)
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  • Johansson, J, et al. (författare)
  • Molecular effects of proinsulin C-peptide
  • 2002
  • Ingår i: Biochemical and biophysical research communications. - : Elsevier BV. - 0006-291X. ; 295:5, s. 1035-1040
  • Tidskriftsartikel (refereegranskat)
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  • Jonasson, P., et al. (författare)
  • Integrated bioprocess for production of human proinsulin C-peptide via heat release of an intracellular heptameric fusion protein
  • 2000
  • Ingår i: Journal of Biotechnology. - 0168-1656 .- 1873-4863. ; 76:03-feb, s. 215-226
  • Tidskriftsartikel (refereegranskat)abstract
    • An integrated bioprocess has been developed suitable for production of recombinant peptides using a gene multimerization strategy and site-specific cleavage of the resulting gene product. The process has been used for production in E. coli of the human proinsulin C-peptide via a fusion protein BB-C7 containing seven copies of the 31-residues C-peptide monomer. The fusion protein BB-C7 was expressed at high level, 1.8 g l(-1), as a soluble gene product in the cytoplasm. A heat treatment procedure efficiently released the BB-C7 fusion protein into the culture medium. This step also served as an initial purification step by precipitating the majority of the host cell proteins, resulting in a 70% purity of the BB-C7 fusion protein. Following cationic polyelectrolyte precipitation of the nucleic acids and anion exchange chromatography, native C-peptide monomers were obtained by enzymatic cleavage at flanking arginine residues. The released C-peptide material was further purified by reversed-phase chromatography and size exclusion chromatography. The overall yield of native C-peptide at a purity exceeding 99% was 400 mg l(-1) culture, corresponding to an overall recovery of 56%. The suitability of this process also for the production of other recombinant proteins is discussed.
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  • Jornvall, H., et al. (författare)
  • Multiplicity of eukaryotic ADH and other MDR forms
  • 2003
  • Ingår i: Chemico-Biological Interactions. - 0009-2797 .- 1872-7786. ; 143-144, s. 255-261
  • Konferensbidrag (övrigt vetenskapligt/konstnärligt)abstract
    • Eukaryotic genomes code for at least eight medium-chain dehydrogenases/reductases (MDR) enzyme families of two types, with and without Zn2+ at the active site. Four families have Zn2+: 'Dimeric alcohol dehydrogenases (ADHs)' (including liver ADHs), 'Tetrameric ADHs' (including the yeast ADHs), 'Cinnamyl ADHs' and 'Polyol DHs'. In the human genome, there are minimally 23 MDR genes, but the list is still growing from further interpretations. Of these, seven genes on chromosome 4 (and three pseudogenes) represent the ADH classes in the gene order IV, I?, Iß, Ia, V, II and III. The lineages leading to human ADH establish five levels of divergence, with nodes at the MDR/short-chain dehydrogenases/reductases (SDR), dimer/tetramer, class III/non-III, further class, and intraclass levels of divergence. These multiplicities allow conclusions on pathways of function for ADHs and suggest this activity to have two roles in addition to its function in metabolism, one of a basic defence nature, the other of regulatory value in higher eukaryotes. © 2002 Elsevier Science Ireland Ltd. All rights reserved.
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  • Jornvall, H, et al. (författare)
  • Pharmacogenetics of the alcohol dehydrogenase system
  • 2000
  • Ingår i: Pharmacology. - : S. Karger AG. - 0031-7012 .- 1423-0313. ; 61:3, s. 184-191
  • Tidskriftsartikel (refereegranskat)abstract
    • Alcohol dehydrogenase (ADH) constitutes a complex enzyme system with different forms and extensive multiplicity. A combination of constant and variable properties regarding function, multiplicity and structure of ADH is highlighted for the human system and extended to ADH forms in general. Future perspectives suggest continued studies in specific directions for distinction of metabolic, regulatory and pharmacogenetic roles of ADH.
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  • Resultat 1-50 av 89

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