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  • 1
    Electronic Resource
    Electronic Resource
    Iron(III) species formed during iron(II) oxidation and iron-core formation in the bacterioferritin ofEscherichia coli (1996)
    Springer
    Il nuovo cimento della Società Italiana di Fisica 18 (1996), S. 347-352 
    Details
    ISSN: 0392-6737
    Keywords: Mössbauer effect ; other γ-ray spectroscopy ; Other topics in biophysics and medical physics ; Conference proceedings
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Summary This paper describes a preliminary investigation of the mechanisms of Fe(II) oxidation and storage of Fe(III) in the bacterioferritin ofEscherichia coli (EcBFR). Using Mössbauer spectroscopy to examine the initial oxidation of iron by EcBFR we have confirmed that this ferritin exhibits «ferroxidase» activity and have shown that dimeric and monomeric iron species are produced as intermediates. We compare the characteristics of ferroxidase activity in EcBFR with those of human H-chain ferritin (HuHF) and discuss the different Mössbauer parameters of their dimeric iron with reference to the structures of their di-metal sites. In addition, we present preliminary findings suggesting that after an initial «burst», the rate of oxidation is greatly reduced, possibly due to blockage of the ferroxidase centre by bound iron. A new component, not found in HuHF and probably representing a small cluster of Fe(III) atoms, is reported.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02458916
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  • 2
    Electronic Resource
    Electronic Resource
    Theα isoform of protein kinase C inhibits histamine-stimulated adenylate cyclase activity in a particulate fraction of the human gastric cancer cell line HGT-1 (1995)
    Springer
    Inflammation research 44 (1995), S. 66-69 
    Details
    ISSN: 1420-908X
    Keywords: Adenylate cyclase ; Protein kinase C ; Histamine H2 receptor ; Stomach
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The isoform of protein kinase C responsible for the inhibition of histamine-stimulated adenylate cyclase by the phorbol ester, 12-O-tetradecanoylphorbol 13-acetate (TPA), has been investigated in a particulate fraction prepared from the human gastric cancer cell line HGT-1. Theα and∈ isoforms of protein kinase C were detected in HGT-1 cells and in a 40,000 × g particulate fraction by immunoblotting procedures. The inhibitory effect of TPA on histamine-stimulated adenylate cyclase was enhanced by the presence of Ca2+, but decreased in a concentrationdependent manner by anti-peptide antibody to protein kinase Cα, but not to protein kinase C∈. Addition of Ca2+ and TPA to the 40,000 × g particulate fraction stimulated the phosphorylation of the protein kinase C substrate myelin basic peptide 4–14. Protein kinase Cα is probably the isoform responsible for inhibition of histamine-stimulated adenylate cyclase in HGT-1 cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01793214
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    Paper (German National Licenses)
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