Abstract
IT has been shown by paper electrophoresis that xanthine dehydrogenase activity is bound to the globulin fractions of rat serum1. Using differential centrifugation, it was demonstrated that xanthine oxidase and xanthine dehydrogenase activities are present in the supernatant fluid corresponding to the ‘cell sap’ containing the soluble proteins of the rat liver2.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Mitidieri, E., Ribeiro, L. P., Affonso, O. R., and Villela, G. G., Biochim. Biophys. Acta, 17, 587 (1955).
Villela, G. G., Mitidieri, E., and Affonso, O. R., Nature, 175, 1087 (1955).
Adjutantis, G., Nature, 173, 539 (1954).
Hogeboom, G. H., Schneider, W. C., and Pallade, G. E., J. Biol. Chem., 172, 619 (1948).
Roush, A., and Norris, E. R., Arch. Biochem., 29, 344 (1950).
Villela, G. G., Rev. Brasil. Biol., 14, 455 (1954).
Svedberg, T., and Pedersen, K. O., “The Ultracentrifuge”, 296 (Oxford, 1940).
Villela, G. G., and Mitidieri, E., Nature, 175, 208 (1955).
Affonso, O. R., Mitidieri, E., Ribeiro, L. P., and Villela, G. G., Proc. Soc. Exp. Biol. Med., 90, 527 (1955).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
MITIDIERI, E., AFFONSO, O., RIBEIRO, L. et al. Detection of Xanthine Dehydrogenase Activity in Soluble Proteins of Rat Liver separated by Paper Electrophoresis. Nature 178, 492–493 (1956). https://doi.org/10.1038/178492b0
Issue Date:
DOI: https://doi.org/10.1038/178492b0
This article is cited by
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.