Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 13 October 1972:
Vol. 178. no. 4057, pp. 172 - 174
DOI: 10.1126/science.178.4057.172
Prev | Table of Contents | Next

Articles

Thyroxine-Binding Globulin: Specificity for the Hormonally Active Conformation of Triiodothyronine

George C. Schussler 1

1 Department of Medicine, State University of New York, Buffalo 14203

The conformational requirements for binding of triiodothyronine to thyroxine-binding globulin were investigated with triiodothyronine analogs having restricted rotation at the ether bond. Although it has been reported that the predominant conformation of triiodothyronine carries the 3' iodine in a position proximal to the phenylalanine ring, the analog for the distal, hormonally active orientation of the 3' iodine is more effective in displacing triiodothyronine and thyroxine from thyroxine-binding globulin. The lower binding affinity of thyroxine-binding globulin for triiodothyronine as compared to thyroxine may be explained by specificity of the binding site for the less abundant conformation of triiodothyronine.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Distal Conformation of the Thyroid Hormone 3,5,3'-Triiodo-L-Thyronine.
V. Cody and W. L. Duax (1973)
Science 181, 757-758
   Abstract »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)