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  • glutathione  (1)
  • passive uptake  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Copper uptake and intracellular distribution in the human intestinal Caco-2 cell line (2000)
    Springer
    BioMetals 13 (2000), S. 179-185 
    Details
    ISSN: 1572-8773
    Keywords: GSH ; heavy metals ; metallothionein ; passive uptake ; 64Cu
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The apical uptake of 64CuCl2 was investigated in human differentiated intestinal Caco-2 cells grown on permeable supports. At pH 6.0 in the apical compartment, the uptake of copper was linear over the first 6 min and between 10 and 80 μM CuCl2 exhibited non-saturable transport kinetics. In addition, copper uptake was energy-independent, affected by the valency state of copper, preferring Cu(II) over Cu(I), and not influenced by high (10 mM) extracellular calcium. The intracellular distribution of copper was investigated by FPLC at different times of uptake (`pulse') and of `chase'. Intracellular copper initially bound predominantly to low molecular weight components (i.e., glutathione), and subsequently shifted to higher molecular weight components such as metallothionein and Cu,Zn superoxide dismutase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009271622356
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  • 2
    Electronic Resource
    Electronic Resource
    Copper-glutathione complexes under physiological conditions: structures in solution different from the solid state coordination (1996)
    Springer
    BioMetals 9 (1996), S. 3-9 
    Details
    ISSN: 1572-8773
    Keywords: copper complexes ; copper transport ; ESR spectroscopy ; glutathione
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The physiologically important copper complexes of oxidized glutathione have been examined by electron spin resonance (ESR) spectroscopy in aqueous solution at neutral pH. Low temperature measurements show that the Cu(II) binding site in oxidized glutathione has the same ligand arrangement as in the copper complexes of S-methylglutathione, glutamine, glutamate and glycine. The site is composed of the amino nitrogens and the carboxyl oxygens of two γ-glutamyl residues; there is no interaction with amide nitrogens, the sulphur bond or the glycyl carboxyl groups. At high metal to ligand ratios a binuclear species exists, in which each Cu(II) binds only to one γ-glutamyl residue. The previously reported forbidden transition detected at g = 4 is due to non-specific aggregation and not to spin coupling of intramolecular sites. Liquid solution ESR spectra show the Cu(II)-glutathione complex has a lower mobility than the corresponding Cu(II)-S'-methylglutathione species. From the degree of spectral anisotropy the complex with glutathione is calculated to exist as a dimer. These results demonstrate that the physiologically relevant complex between copper and oxidized glutathione in solution is completely different from the known solid state structure determined by crystallography.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00188083
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