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  • 1
    Electronic Resource
    Electronic Resource
    High affinity receptors for vasoactive intestinal peptide on a human glioma cell line
    Amsterdam : Elsevier
    Peptides 11 (1990), S. 1225-1231 
    Details
    ISSN: 0196-9781
    Keywords: Binding specificity ; Degradation ; Human glioma cells ; Internalization ; Vasoactive intestinal peptide receptors
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0196-9781(90)90156-Y
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Receptor binding and biological effect of insulin in human adipocytes (1977)
    Springer
    Diabetologia 13 (1977), S. 589-593 
    Details
    ISSN: 1432-0428
    Keywords: Insulin receptors ; human adipocytes ; insulin degradation ; lipogenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The binding of125I-labelled insulin to human adipocytes was studied at 37° C. The precipitability of the125I-labelled insulin preparation (0.03 nmol/l) in trichloroacetic acid and the concentration of biologically active insulin (7.5 nmol/l) remained constant in buffer incubated with human adipocytes (100 μl cells/ml suspension) for 30–60 minutes at 37° C, whereas more than half of the insulin was inactivated by rat fat cells under the same conditions. A constant level of binding of125I-labelled insulin (0.03 nmol/l) to human adipocytes was obtained after 45 minutes. The apparent dissociation constant of receptor binding was about 0.2 nmol/l as compared to about 2 nmol/l for rat adipocytes. Conversion of [U-14C]glucose to lipids was stimulated half-maximally by about 0.05 nmol/l of insulin (similar to rat adipocytes). Thus, half-maximal stimulation of human adipocytes was obtained with a receptor occupancy of about 20–30 per cent.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01236312
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Insulin receptors: Structure and function (1986)
    Springer
    Cellular and molecular life sciences 42 (1986), S. 727-734 
    Details
    ISSN: 1420-9071
    Keywords: Insulin receptors ; subunits ; phosphorylation ; serine kinase ; tyrosine kinase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary and conclusions The recent characterization of the human insulin receptor structure and its intrinsic tyrosine kinase activity represent major advances in our understanding of the mechanism of insulin action. It is reasonable to think that the insulin-induced autophosphorylation and activation of its receptor kinase represent an important event in the action of insulin on cell metabolism and growth. The fundamental research reviewed may be followed by the discovery of molecular receptor defects in clinical syndromes of insulin resistance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01941518
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    Paper (German National Licenses)
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