Abstract
DURING the enzymic de-iodination of thyroxine labelled with iodine-131, triiodothyronine and related compounds with tissue homogenates, a fraction of the radioactivity consistently appeared in a material of RF = 0 in various chromatographic systems1. The amount of ‘origin’ radioactive material found on chromatograms increased almost in parallel with the de-iodination of the substrate. With the identification of ferrous ions and flavin as activators for thyroxine dehalogenase2, the formation of this material was found to be dependent only on flavin derivatives. The nature of the ‘origin’ iodine-131 labelled material was studied with purified preparations of thyroxine dehalogenase3 ; it was found to be radioiodinated protein(s) present in the tissue enzymic extracts, as described below.
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
Tata, J. R., Rall, J. E., and Rawson, R. W., Endocrinol., 60, 83 (1957) ; Proc. Soc. Exp. Biol., N.Y., 95, 362 (1957).
Tata, J. R., Biochim. Biophys. Acta, 35, 567 (1959).
Tata, J. R., Biochem. J. (in the press).
Saunders, B. C., and Stark, B. P., Tetrahedron, 4, 169 (1958).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
TATA, J. Transiodination of Proteins during Enzymic De-iodination of Thyroxine. Nature 187, 1025–1026 (1960). https://doi.org/10.1038/1871025a0
Issue Date:
DOI: https://doi.org/10.1038/1871025a0
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.