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  • 1985-1989  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    Interaction of thymic peptide thymosinα 1 with vasoactive intestinal peptide (VIP) receptors (1986)
    Springer
    Bioscience reports 6 (1986), S. 727-733 
    Details
    ISSN: 1573-4935
    Keywords: Thymosin ; vasoactive intestinal peptide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Thymic peptide thymosin α1 (10−9 to 3 x 1010−7 M) is shown to inhibit the specific binding of [125I]VIP to rat blood mononuclear cells and liver plasma membranes. Thymosin α1 was 160 and 6250 times less potent that VIP at inhibiting [125I]VIP binding to blood mononuclear cells and liver plasma membranes, respectively. Thymosin α1 (10−10 to 1010−7 M) was weak in stimulating adenylate cyclase activity. Its efficacy is about 25 % and 27 % that of native VIP in blood mononuclear cells and liver plasma membranes, respectively. Thymosin α1 may behave as a partial VIP agonist in rat.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01116540
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Vasoactive intestinal peptide (VIP) binding to solubilized material from rat liver plasma membranes (1986)
    Springer
    Bioscience reports 6 (1986), S. 39-44 
    Details
    ISSN: 1573-4935
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A non-ionic detergent such as Lubrol-PX extracts in soluble form the VIP-binding structures of rat liver plasma membranes. Detergent-solubitized proteins bind specifically [125I]VIP and the complex tracer-protein is identified by the use of Sepharose 6B columns. The interaction is only possible in the absence of detergent (below 0.001%) and is inhibited by native peptide. A molecular weight of about 80,000 was estimated for VIP-binding proteins by reference to a series of globular markers of proteins. Binding to VIP soluble proteins is specific and dependent on time as studied by the Hummel and Dreyer (Biochim. Biophys. Acta 63:530–532, 1962) assay.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01145177
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  • 3
    Electronic Resource
    Electronic Resource
    Interaction of a bovine thymic peptide extract with vasoactive intestinal peptide (VIP) receptors (1986)
    Springer
    Bioscience reports 6 (1986), S. 579-584 
    Details
    ISSN: 1573-4935
    Keywords: Vasoactive intestinal peptide (VIP) ; thymic peptides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Bovine t hymic peptide extract (1–100 μg/ml) is shown to completely inhibit the binding of [125I]VIP to rat blood mononuclear cells, lymphoid cells of spleen, and liver plasma membranes. In the three models, the bovine thymic peptide extract inhibits [125I]VIP binding with a potency that is 4000–7000 times lower than that of the native VIP, on a weight basis. In rat liver plasma membranes, the bovine thymic peptide extract stimulates adenylate cyclase with a maximal efficiency that is similar to that of VIP. At maximal doses, VIP and thymic peptide extract do not exert an additive effect on adenylate cyclase, suggesting that the activation of the enzyme by the bovine thymic peptide extract occurs through VIP receptors. Finally, no VIP-like immunoreactivity was detected in the thymic peptide extract using an antiserum raised against mammalian VIP. All these data suggest the presence in the bovine thymic peptide extract of a new substance which behaves as a VIP agonist in rat.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01114955
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    Paper (German National Licenses)
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