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.

Inhibitory Effect of ‘Diamox’ and Chloroquine on the NADH2-Monodehydroascorbic Acid-transhydrogenase Activity of Retinal and Ciliary Microsomes

Nature volume 202, pages 1128–1129 (1964)Cite this article

Abstract

CYANIDE-INSENSITIVE, ascorbic acid-dependent NADH2 oxidation has recently been demonstrated in plant1,2 and animal3 tissues. It has been postulated3 that ascorbic acid is oxidized by cytochrome b5 to monodehydroascorbic acid, which is later reduced to ascorbic acid by NADH2-monodehydroascorbic acid-transhydrogenase. As the oxygen uptake of the retina4, ciliary body5, lens6 and cornea7 is not completely inhibited by cyanide and these tissues all contain high levels of ascorbic acid8, it was decided to investigate the occurrence of this enzyme in ocular tissues.

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

Access options

Rent or buy this article

Get just this article for as long as you need it

$39.95

Learn more

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

References

  1. Nason, A., Wosilait, W. D., and Terrell, A. J., Arch. Biochem. Biophys., 48, 233 (1954).

    Article  CAS  Google Scholar 

  2. Kern, M., and Racker, E., Arch. Biochem. Biophys., 48, 235 (1954).

    Article  CAS  Google Scholar 

  3. Staudinger, Hj., Krisch, K., and Leonhäuser, S., Ann. N.Y. Acad. Sci., 92, 195 (1961).

    Article  ADS  CAS  Google Scholar 

  4. Robbie, W. A., and Leinfelder, P. J., Arch. Biochem., 16, 437 (1948).

    CAS  PubMed  Google Scholar 

  5. DeRoetth, A., Arch. Ophthal., 50, 491 (1953).

    Article  Google Scholar 

  6. Kinoshita, J. H., Arch. Ophthal., 54, 360 (1955).

    Article  CAS  Google Scholar 

  7. Hermann, H., Moses, S. G., and Friedenwald, J. S., Arch. Ophthal., 28, 652 (1942).

    Article  Google Scholar 

  8. Heath, H., Exp. Eye Res., 1, 362 (1962).

    Article  CAS  Google Scholar 

  9. Strittmatter, C. F., and Ball, E. G., Proc. U.S. Nat. Acad. Sci., 38, 19 (1952).

    Article  ADS  CAS  Google Scholar 

  10. Wetterholm, D. H., and Winter, F. C., Arch. Ophthal., 71, 82 (1964).

    Article  CAS  Google Scholar 

  11. Datta, A., and Basu, U., J. Sci. Indust. Res., 14C, 61 (1955).

    Google Scholar 

  12. Friedenwald, J. S., Buschke, W., and Michel, H. O., Arch. Ophthal., 29, 535 (1943).

    Article  CAS  Google Scholar 

  13. Tormey, J. McD., J. Cell Biol., 17, 641 (1963).

    Article  CAS  Google Scholar 

  14. Holmberg, A., Arch. Ophthal., 62, 935 (1959).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Chemical Pathology, University College Hospital Medical School, London, W.C.1

    H. HEATH & ROSEMARY FIDDICK

Authors
  1. H. HEATH
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. ROSEMARY FIDDICK
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and Permissions

About this article

Cite this article

HEATH, H., FIDDICK, R. Inhibitory Effect of ‘Diamox’ and Chloroquine on the NADH2-Monodehydroascorbic Acid-transhydrogenase Activity of Retinal and Ciliary Microsomes. Nature 202, 1128–1129 (1964). https://doi.org/10.1038/2021128a0

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1038/2021128a0

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

Advanced 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