Literature DB >> 5420146

Lack of antagonism between thioglycerol and an oxytocin analogue not containing a disulphide bond.

H O Schild.   

Abstract

1. The antagonistic effect of thioglycerol against oxytocin and an analogue of oxytocin not containing a disulphide bridge (desamino-1-carba-oxytocin) has been compared in the rat isolated depolarized uterus.2. Thioglycerol clearly differentiated between the two compounds, 40 mM producing a dose ratio of 12 with oxytocin but only 1.5 with the carba compound.3. It was confirmed that thioglycerol produces no appreciable destruction of oxytocin in vitro.4. The mode of action of thiols in antagonizing specifically S-S polypeptides is discussed. It is concluded that they probably do not produce their effect either by inactivating receptors or by inactivating S-S polypeptides in solution. A possible mechanism is that thiols potentiate the destruction of S-S polypeptides at the receptor site.

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Year:  1970        PMID: 5420146      PMCID: PMC1702942     

Source DB:  PubMed          Journal:  Br J Pharmacol        ISSN: 0007-1188            Impact factor:   8.739


  3 in total

1.  [Mechanism of the inactivation of oxytocin by uterine tissue].

Authors:  L AUDRAIN; H CLAUSER
Journal:  Biochim Biophys Acta       Date:  1960-03-11

2.  The antagonism of disulphide polypeptides by thiols.

Authors:  P J Martin; H O Schild
Journal:  Br J Pharmacol Chemother       Date:  1965-10

3.  The effect of metals on the S-S polypeptide receptor in depolarized rat uterus.

Authors:  H O Schild
Journal:  Br J Pharmacol       Date:  1969-06       Impact factor: 8.739

  3 in total
  1 in total

1.  Inhibition of Escherichia coli by thioglycerol.

Authors:  K K Jensen; G T Javor
Journal:  Antimicrob Agents Chemother       Date:  1981-04       Impact factor: 5.191

  1 in total

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