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  • 1995-1999
  • 1985-1989  (4)
  • 1989  (4)
Material
Years
  • 1995-1999
  • 1985-1989  (4)
Year
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 52 (1989), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The murine neuroblastoma N1E-115 cell line contains binding sites for the angiotensin II (Ang II) receptor antagonist 125I-[Sarc1,Ile8]-Ang II (125I-SARILE). Binding of 125I-SARILE to N1E-115 membranes was rapid, reversible, and specific for Ang II-related peptides. The rank order potency of 125I-SARILE binding was the following: [Sar1]-Ang II = [Sar1Ile8]-Ang II 〉 Ang II 〉 Ang III = [Sarc1, Thr8]-Ang II 〉 Ang I. Scatchard analysis of membranes prepared from confluent monolayers revealed a homogenous population of high affinity (KD= 383 ± 60 pM) binding sites with aBmax of 25.4 ± 1.6 fmol/mg of protein. Moreover, the density, but not the affinity, of the binding sites increased as the cells progressed from logarithmic to stationary growth in culture. Finally, agonist, but not antagonist, binding to N1E-115 cells was regulated by guanine nucleotides. Collectively, these results suggest that the murine neuroblastoma N1E-115 cell line may provide a useful model in which to investigate the signal transduction mechanisms utilized by neuronal Ang II receptors.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Environmental science & technology 23 (1989), S. 1438-1443 
    ISSN: 1520-5851
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Energy, Environment Protection, Nuclear Power Engineering
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 3
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    Unknown
    Cambridge, Mass., etc., : Periodicals Archive Online (PAO)
    Greek, Roman and Byzantine Studies. 30:3 (1989) 451 
    Library Location Call Number Volume/Issue/Year Availability
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 112 (1989), S. 59-66 
    ISSN: 1432-1424
    Keywords: parachloromercuribenzoic acid ; Cl/OH exchange ; sulfhydryl reagents ; chloride transport ; DIDS ; brush-border membranes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The effect of the sulfhydryl reagent parachloromercuribenzoic acid (PCMB) on chloride transport was examined in rabbit renal brush-border membrane vesicles (BBMV). PCMB had no effect on the chloride conductive pathway. In the presence of an inside-alkaline pH gradient and a K+/valinomycin voltage clamp, the addition of PCMB stimulated36Cl uptake and induced a threefold overshoot above the equilibrium value, indicating Cl/OH exchange. The effect of PCMB was reversed by dithiothreitol. Cl/OH exchange was not observed in the absence of PCMB. PCMB-activated Cl/OH exchange persisted even when the membrane potential was made inside-negative relative to the controls, thus, demonstrating that PCMB's effect on36Cl uptake under pH-gradient conditions is not mediated by parallel Cl− and H+ conductive pathways. PCMB-activated Cl/OH exchange was inhibited by 4,4′-diisothiocyanostilbene-2,2′-disulfonic acid (DIDS) and 5-nitro-2-(3-phenylpropylamino)-benzoic acid (NPPB) with IC50 values of 290 and 80 μm, respectively. These results demonstrate that modification of sulfhydryl groups by PCMB activates Cl/OH exchange in BBMV.
    Type of Medium: Electronic Resource
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