Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Letter
  • Published:

Inhibition of Chemi-luminescence of Luminol by means of Oximes

Abstract

IT is known that oximes with widely different chemical structures are effective reactivators of cholinesterase inhibited by organo-phosphorous compounds (esters of phosphoric or thiophoric acid, insecticides, nerve gases)1. The mechanism of this reaction is considered to be due to the chemical interaction of oximes with the free or bound ester of phosphoric acid, which is hydrolysed by the oxime2, and is not available for the inhibition of the cholinesterase. It is known that organo-phosphorous compounds catalyse the luminol reaction causing an intensive chemi-luminescence of luminol (3-amino-phthalylhydrazide) in alkaline medium in the presence of sodium perborate as oxygen donor3.

This is a preview of subscription content, access via your institution

Access options

Buy this article

Prices may be subject to local taxes which are calculated during checkout

Similar content being viewed by others

References

  1. Davies, D. R., and Greeb, A. L., Brit. J. Industr. Med., 16, 128 (1959). Holmstedt, B., Pharmacol. Rev., 11, 567 (1959).

    CAS  PubMed  Google Scholar 

  2. Green, A. L., and Sasille, B., J. Chem. Soc., 3887 (1956).

  3. Goldenson, J., Anal. Chem., 29, 877 (1957).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

WEBER, K., MATKOVIĆ, J. & FLEŠ, D. Inhibition of Chemi-luminescence of Luminol by means of Oximes. Nature 191, 177–178 (1961). https://doi.org/10.1038/191177a0

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1038/191177a0

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.

Search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing