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  • 1985-1989  (2)
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Year
  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 48 (1987), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The pattern of hydrolysis of [3H]angiotensin II ([3H]AII; 20 nM) by intact cells was studied on cultured mouse spinal cord cells. Degradation products were identified by HPLC analysis after incubation for 2 h at 37°C. In the absence of peptidase inhibitors, 70% of [3H]AII was degraded, and the main labeled metabolite was [3H]tyrosine (40% of total radioactivity). Minor quantities of [3H]AII1–5 and [3H]AII4–8 were formed. Results obtained in the presence of various inhibitors indicate that several enzymes were involved in the All-hydrolyzing process. Dipeptidyl aminopeptidase III (EC 3.4,14.4) could play a critical role, as suggested by the formation of [3H]Val3-Tyr4 and [3H]-Tyr4-IIe5 in the presence of bestatin (2 ± 10−5M). This hypothesis was confirmed by the potency of dipeptidyl aminopeptidase III inhibitors to inhibit both [3H]AII hydrolysis and formation of these 3H-labeled dipeptides. An arylamidase-like activity could also be participating in [3H]AII hydrolysis, because higher concentrations of bestatin (10−4M) in association with dipeptidyl aminopeptidase III inhibitors totally inhibited [3H]tyrosine formation, increased protection of [3H]AII and [3H]AII1–7 formed, and provoked a slight accumulation of [3H]AII2–8. These results suggest that the formation of [3H]AII2–8 is due to the action of a bestatininsensitive acidic aminopeptidase and that the Pro7-Phe8 cleavage is also a step of AII hydrolysis, resulting from the action of an unidentified peptidase different from prolyl endopeptidase. Because care was taken to eliminate interference by enzymes leaking out into the incubation medium, the AII-hydrolyzing process described on these cultured mouse spinal cord cells presumably occurs under the action of membrane-bound peptidases.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of metamorphic geology 3 (1985), S. 0 
    ISSN: 1525-1314
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Geosciences
    Notes: Abstract Chemical analysis (including H2, F2, FeO, Fe2O3) of a Mg-vesuvianite from Georgetown, Calif., USA, yields a formula, Ca18.92Mg1.88Fe3+0.40Al10.97Si17.81- O69.0.1(OH)8.84F0.14, in good agreement on a cation basis with the analysis reported by Pabst (1936). X-ray and electron diffraction reveal sharp reflections violating the space group P4/nnc as consistent with domains having space groups P4/n and P4nc. Refinement of the average crystal structure in space group P4/nnc is consistent with occupancy of the A site with Al, of the half-occupied B site by 0.8 Mg and 0.2 Fe, of the half-occupied C site by Ca, of the Ca (1,2,3) sites by Ca, and the OH and O(10) sites by OH and O. We infer an idealized formula for Mg-vesuvianite to be Ca19Mg(MgAl7)Al4Si18O69(OH)9, which is related to Fe3+-vesuvianite by the substitutions Mg + OH = Fe3++ O in the B and O(10) sites and Fe3+= Al in the AlFe site.Thermodynamic calculations using this formula for Mg-vesuvianite are consistent with the phase equilibria of Hochella, Liou, Keskinen & Kim (1982) but inconsistent with those of Olesch (1978). Further work is needed in determining the composition and entropy of synthetic vs natural vesuvianite before quantitative phase equilibria can be dependably generated. A qualitative analysis of reactions in the system CaO-MgO-Al2O3-SiO2-H2O-CO2 shows that assemblages with Mg-vesuvianite are stable to high T in the absence of quartz and require water-rich conditions (XH2O 〉 0.8). In the presence of wollastonite, Mg-vesuvianite requires very water-rich conditions (XH2O 〉 0.97).
    Type of Medium: Electronic Resource
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