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  • 1H NMR Tautomerism  (1)
  • Conference proceedings  (1)
  • Histamine H2 receptor  (1)
  • Mössbauer spectroscopy  (1)
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  • 1
    Digitale Medien
    Digitale Medien
    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
    Schlagwort(e): Adenylate cyclase ; Protein kinase C ; Histamine H2 receptor ; Stomach
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01793214
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  • 2
    Digitale Medien
    Digitale Medien
    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
    Schlagwort(e): Mössbauer effect ; other γ-ray spectroscopy ; Other topics in biophysics and medical physics ; Conference proceedings
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Physik
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02458916
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  • 3
    Digitale Medien
    Digitale Medien
    Magnetic properties of human liver and brain ferritin (1999)
    Springer
    European biophysics journal 28 (1999), S. 263-267 
    Details
    ISSN: 1432-1017
    Schlagwort(e): Key words Human liver ; Human brain ; Ferritin ; Electron microscopy ; Mössbauer spectroscopy
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Physik
    Notizen: Abstract Human brain (globus pallidus) and liver tissues were investigated by means of electron microscopy (EM), Mössbauer spectroscopy (MS) and SQUID magnetometry techniques. Based on MS measurements, the iron present was identified to be in the ferritin-like form (61–88%) and in the form of a low-spin iron species (the balance). Its overall concentration was estimated as 1.5(3) mg in the brain and 2.4(5) mg in the liver, per gram of lyophilized tissue. The average core diameter was determined by EM measurements to be equal to 7.5(1.3) nm for the liver and 3.3(5) nm for the brain. Magnetization measurements carried out between 5 and 300 K yielded an estimation of an average blocking temperature, KT BL, as equal to 6.7 K and 8.5 K for the liver and the brain, respectively. From the dependence of KT BL on the external magnetic field it was concluded that the ferritin-like cores in the studied samples can be regarded as non-interacting particles. Finally, the uniaxial magnetic anisotropy constant was determined to be 6×103 J/m3 for the liver and 4×104 J/m3 for the brain.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s002490050208
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  • 4
    Digitale Medien
    Digitale Medien
    1H and 13C NMR studies of the protonation of isomeric methoxysulmazole analogues (1990)
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 28 (1990), S. 573-575 
    Details
    ISSN: 0749-1581
    Schlagwort(e): Inotropism ; Imidazopyridine ; 13C NMR ; 1H NMR Tautomerism ; Chemistry ; Analytical Chemistry and Spectroscopy
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: The major protonation sites of six cardiotonic isomeric 2-aryl-n-methoxy-1H-imidazo[4,5-b]- and -[4,5-c]-pyridines (n = 4-7) were determined by 1H and 13C NMR methods. All the 1H-imidazo[4,5-c]pyridines and the 7-methoxy derivative of sulmazole were found to protonate at the pyridyl nitrogen. Protonation occurred at the imidazo nitrogen, however, for the 5- and 6-methoxy derivatives of sulmazole.
    Zusätzliches Material: 2 Tab.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/mrc.1260280703
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