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  • Electronic Resource  (3)
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  • Electronic Resource  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    Analogs of oxytocin with L- and D-pentafluorophenylalanines in the second position (1977)
    Springer
    Chemistry of natural compounds 13 (1977), S. 332-336 
    Details
    ISSN: 1573-8388
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary 1. The separation of pentafluorophenylalanine into optical antipodes has been effected. 2. Two new analogs of oxytocin — [2-L-pentafluorophenylalanine]oxytocin and [2-D-pentafluorophenylalanine]oxytocin — have been synthesized and their uterotonic activities have been studied. 3. It has been shown that donor — acceptor interaction plays a fundamental role in the stimulation of the biological effect.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00573555
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Synthesis of [D-phe3 (NH2); Pro3; D-Ala6]- and [D-Phe2 (NO2); Pro3; D-Ala6]luliberins (1980)
    Springer
    Chemistry of natural compounds 16 (1980), S. 518-524 
    Details
    ISSN: 1573-8388
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract In order to study the influence of substituents of the aromatic ring of D-phenyl-alanine on the inhibiting capacity of luliberian analogs, we have synthesized two new analogs: and luliberin. The synthesis was performed by the fragmentary condensation method using 2+(3+5) and 2+(5+3) schemes. A new and convenient method of obtaining the amide of the C-terminal tetrapeptide of the luliberin sequence has been developed. In the condensation of the fragments, both the azide and the carbodimide method of synthesis with the addition of l-hydroxybenzotriazole were used. The guanidino group of arginine was protected by nitration, while the hydroxy groups of serine and of tyrosine were not protected. The complete elimination of the protective groups from the decapeptides was performed by catalytic hydrogenation over Pd on carbon and by anhydrous HF with the addition of anisole at 0°C. The protected octa- and decapeptides were purified by gel filtration on Sephadex LH-20 in ethanol or by preparative thin-layer chromatography on silica gel plates. The final peptides were purified by ion-ex-exchange chromatography on Sephadex CM-25.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00571054
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Synthetic analog of the thymosinα1 fragment 24–28 alters the coagulating and aggregating activities of α-thrombin (1995)
    Springer
    Bulletin of experimental biology and medicine 120 (1995), S. 671-674 
    Details
    ISSN: 1573-8221
    Keywords: thrombin ; thymosin ; platelets ; blood coagulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract A pentapeptide (EEAEN), which is the 24–28 fragment of the COOH-terminal sequence in the thymosinα1 molecule highly homologous with the 54–58 region of hirudin (with the complementary anion-binding exosite in the thrombin molecule), was synthesized by a solid-phase method. Preincubation of α-thrombin with EEAEN in concentrations of 0.1 pM to 1 nM reduced its clotting activity while preincubation of this enzyme with EEAEN in concentrations of 0.01 to 1 nM reduced its platelet-aggregating activity. The reaction of EEAEN with thrombin is shown to be similar to the reaction of the entire thymosinα1 molecule. It is concluded that the COOH-terminal thymosinα1 peptide EEAEN may be the reactive site responsible for the antithrombin activity of thymosinα1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02444656
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    Paper (German National Licenses)
    Fulltext
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