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  • Cross-inhibition analysis  (3)
  • SaOS-2 osteoblast-like cells  (2)
  • uniform particles  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Characterization of amino-acid transport systems in guinea-pig intestinal brush-border membrane
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 985 (1989), S. 120-126 
    Details
    ISSN: 0005-2736
    Keywords: (Guinea-pig intestine) ; Amino acid transport ; Brush-border membrane vesicle ; Cross-inhibition analysis
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0005-2736(89)90355-6
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Characterization of amino acid transport systems in human placental brush-border membrane vesicles
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 904 (1987), S. 309-318 
    Details
    ISSN: 0005-2736
    Keywords: (Human placenta) ; Amino acid transport ; Brush-border membrane vesicle ; Cross-inhibition analysis
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2736(87)90380-4
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of amino acid transport systems in human placental basal membrane vesicles
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 1021 (1990), S. 169-174 
    Details
    ISSN: 0005-2736
    Keywords: (Human placenta) ; Amino acid transport ; Basal membrane vesicle ; Cross-inhibition analysis
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2736(90)90030-R
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    The regulation of L-proline transport by insulin-like growth factor-I in human osteoblast-like SaOS-2 cells (1996)
    Springer
    Pflügers Archiv 432 (1996), S. 419-425 
    Details
    ISSN: 1432-2013
    Keywords: Key words Amino acid transport ; Insulin-like growth factor-I ; SaOS-2 osteoblast-like cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The effect of insulin-like growth factor-I on amino acid transport was studied by measuring the uptake of tritiated L-proline in the cultured human osteoblast-like SaOS-2 cells. The uptake of L-proline was supported by both transport system A, ASC and Gly and by Na+-dependent amino acid transport system A, and by Na+-independent system L. The initial rate of total L-proline uptake as a function of concentration showed saturation and obeyed Michaelis-Menten kinetics with Michaelis constant (K m) and maximum velocity (V max) values of 1.87 mM and 8.89 nmol⋅(mg protein)−1⋅(3 min)−1, respectively. Na+-dependent L-proline uptake was significantly stimulated by insulin-like growth factor-I in a time- and concentration-dependent manner. Kinetic analysis showed that insulin-like growth factor-I enhanced transport activity by increasing the V max of transport without significant changes in the affinity (K m) of the carrier for the substrate. The increase in transport activity was significantly reduced by cycloheximide. The stimulated increment above basal L-proline uptake was completely inhibited by α-(methylamino) isobutyric acid, suggesting that only system A was affected by insulin-like growth factor-I. Na+-dependent L-proline uptake was also stimulated by insulin-like growth factor-II and insulin-like growth factor-I analogues. The insulin-like growth factor-I-stimulated L-proline uptake was inhibited by one of its binding protein, insulin-like growth factor binding protein-4, in a concentration-dependent manner.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004240050153
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  • 5
    Electronic Resource
    Electronic Resource
    The regulation of type-I collagen synthesis by insulin-like growth factor-I in human osteoblast-like SaOS-2 cells (1996)
    Springer
    Pflügers Archiv 433 (1996), S. 123-128 
    Details
    ISSN: 1432-2013
    Keywords: Key words Type-I collagen ; Insulin-like growth factor-I ; SaOS-2 osteoblast-like cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  The effect of insulin-like growth factor-I on collagen synthesis was studied using cultured human osteoblast-like SaOS-2 cells by measuring the incorporation of tritiated L-proline into immunoprecipitable type-I collagen. Tritiated L-proline incorporation into collagen was significantly stimulated by insulin-like growth factor-I in a time- and concentration-dependent manner. Unlabelled L-proline and α-(methylamino) isobutyric acid inhibited either the influx into cells, or the incorporation into collagen, of tritiated L-proline. The increase in incorporation of tritiated L-proline was significantly reduced by cycloheximide and actinomycin D. L-Proline incorporation into collagen was also stimulated by insulin-like growth factor-II, insulin-like growth factor-I analogues and insulin. The insulin-like growth factor-I-stimulated L-proline incorporation was inhibited by one of its binding proteins, insulin-like growth factor binding protein-4, in a concentration-dependent manner.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004240050257
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  • 6
    Electronic Resource
    Electronic Resource
    Formation of uniform silver particles from bis (1,2-ethanediamine)silver(I) complex (1991)
    Springer
    Colloid & polymer science 269 (1991), S. 187-192 
    Details
    ISSN: 1435-1536
    Keywords: Silver particles ; uniform particles ; silver(I) complex ; 1,2-ethanediamine ; surface characterization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Uniform spherical silver particles were produced by decomposing the bis(1,2-ethanediamine)silver(I) complex, by aging a solution of 1.0×10−3 mole dm−3 in silver (I) nitrate, 1.0 mole dm−3 in 1,2-ethanediamine, and 2.5×10−1 mole dm−3 in nitric acid (basic solution) at 100°C for 42 min. The average modal diameter was estimated to be 0.52 μm with a relative standard deviation of 0.10. A moderately oxygenrich layer, ∼40 Å thick, on the surface of the particles was detected by means of photoelectron surface microanalysis (XPS). The silver particles grew through a polynuclear-layer mechanism, as judged from the concentration change in soluble silver(I) species in the supernatant solution. The particles' point of zero charge (PZC) was estimated at pH 6.5 by potentiometric titration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00660310
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  • 7
    Electronic Resource
    Electronic Resource
    Preparation of uniform spherical aluminum hydrous oxide particles from acetylacetonato-aluminum solutions (1991)
    Springer
    Colloid & polymer science 269 (1991), S. 290-294 
    Details
    ISSN: 1435-1536
    Keywords: Aluminum hydrous oxide ; uniform particles ; forced hydrolysis ; aluminum complex ; acetylacetone
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Uniform spherical particles of amorphous aluminum hydrous oxide (0.45 μm in diameter with a relative standard deviation of 0.09) were produced under a limited set of conditions in an aluminum sulfate/acetylacetone system at 100°C aged for 24 h. Grain-like crystalline α-AlOOH particles (2.6 μm in length with a relative standard deviation of 0.10) were also prepared in the absence of sulfate ions at 100°C for 42 h. Their morphology and size were sensitive to the total aluminum concentration, even though the initial pH was kept the same. The temperature dependence of the absorption spectra of acetylacetonato-aluminum complexes indicated their exothermic formation. These complexes release free aluminum ions at elevated temperatures, which subsequently hydrolyzed. The resulting polymerized hydroxo-aluminum species complexes with the sulfate ion act as precursors to particle formation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00665503
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    Paper (German National Licenses)
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