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  • Suramin  (2)
  • Regional brain distribution  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Suramin analogs, divalent cations and ATPγS as inhibitors of ecto-ATPase (1995)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 351 (1995), S. 523-528 
    Details
    ISSN: 1432-1912
    Keywords: Key words Ecto-ATPase ; Suramin ; Metal cation coordination ; ATPγS
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  Ecto-nucleotidases are plasma membrane-bound enzymes that sequentially dephosphorylate extracellular nucleotides such as ATP. This breakdown of ATP and other nucleotides obscures the characterization and classification of P2 (nucleotide) receptors. We therefore studied suramin and several of its analogs, divalent cations and ATPγS for their ability to inhibit ecto-ATPase in human blood cells. Suramin itself and Ni2+ were the more potent, non-competitive inhibitors with micromolar affinity. ATPγS also displayed micromolar affinity and inhibited ecto-ATPase competitively. The data obtained with the divalent cations demonstrate that coordination of the phosphate chain but not the N7 of the adenine ring is required for the breakdown of ATP by ecto-ATPase. Divalent cations that coordinate both the phosphate chain and N7 inhibit ecto-ATPase in a non-competitive manner.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00171044
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    The regional localization of R28935 in the cat brain as dependent on the route of administration (1979)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 309 (1979), S. 281-285 
    Details
    ISSN: 1432-1912
    Keywords: R28935 ; Antihypertensive agents ; Cat brain ; Regional brain distribution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Intravenous injection of the antihypertensive agent R28935 and its pharmacologically less active threo-isomer R29814 resulted in a distribution profile in the cat brain which differed from the regional localization after administration via the left vertebral artery. Although the two isomers had the same physicochemical properties, R28935 penetrated more readily into the CNS. Intravenous administration resulted in almost equal levels in all brain parts, whereas after injection into the vertebral artery caudal structures contained more of both compounds than rostral structures. Differences existed between the concentrations in homotopic brain areas, especially in the brain stem. From comparison of the levels of R28935 after injection of an equiactive dose either i.v. or into the vertebral artery it is tempting to speculate that the mesencephalic tegmentum, the nucleus of the solitary tract, the inferior colliculi and/or the locus coeruleus are possible sites of the hypotensive action.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00504761
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Suramin analogs, divalent cations and ATPγS as inhibitors of ecto-ATPase (1995)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 351 (1995), S. 523-528 
    Details
    ISSN: 1432-1912
    Keywords: Ecto-ATPase ; Suramin ; Metal cation coordination ; ATPγS
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Ecto-nucleotidases are plasma membranebound enzymes that sequentially dephosphorylate extracellular nucleotides such as ATP. This breakdown of ATP and other nucleotides obscures the characterization and classification of P2 (nucleotide) receptors. We therefore studied suramin and several of its analogs, divalent cations and ATPγS for their ability to inhibit ecto-ATPase in human blood cells. Suramin itself and Ni2+ were the more potent, non-competitive inhibitors with micromolar affinity. ATPγS also displayed micromolar affinity and inhibited ecto-ATPase competitively. The data obtained with the divalent cations demonstrate that coordination of the phosphate chain but not the N7 of the adenine ring is required for the breakdown of ATP by ecto-ATPase. Divalent cations that coordinate both the phosphate chain and N7 inhibit ecto-ATPase in a non-competitive manner.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00171044
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
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