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  • Wiley-Blackwell  (2)
  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 53 (1970), S. 63-72 
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The syntheses of seven tripeptide isomers containing L-histidine, L-proline and L-glutamic acid residues, the same as found in the natural thyrotropin-releasing hormone (TRH), are reported. In addition L-pyroglutamyl-L-histidyl-L-proline and its amide as well as Nα-acetyl-L-glutamyl-L-histidyl-L-proline are described. Whereas eight peptides are inactive and L-pyroglutamyl-L-histidyl-L-proline shows a slight TRH activity, L-pyroglutamyl-L-histidyl-L-proline-amide has the full biological activity of the isolated thyrotropin-releasing hormone and, at the present state of knowledge, seems to be identical with it.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 54 (1971), S. 1335-1342 
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The syntheses and biological activities of 4 analogues of the thyrotropin-releasing hormone (TRH) are described. In these analogues the histidine residue has been replaced by L-lysine, L-α,γ-diaminobutyric acid, β-(3-pyrazolyl)-L-alanine, and L-arginine. All analogues exhibited the characteristic biological responses of TRH. For the β-(3-pyrazolyl)-L-alanine analogue as well as for TRH the bioassays suggest an induction of a strong and rapid resynthesis of thyrotropin (TSH) in higher (μg) concentrations.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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