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Science 24 February 1978:
Vol. 199. no. 4331, pp. 904 - 906
DOI: 10.1126/science.622575
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Articles

Science, Vol 199, Issue 4331, 904-906
Copyright © 1978 by American Association for the Advancement of Science

articles

Sulfhydryl groups and the monodeiodination of thyroxine to triiodothyronine

IJ Chopra

Sulfhydryl reagents exert a profound influence on the monodeiodination of thyroxine to triiodothyronine by rat and sheep tissues in vitro. A marked dithiothreitol-induced increase in the monodeiodination by fetal sheep liver homogenates suggests that the characteristically low conversion in fetal tissues is related more to the status of sulfhydryl groups than to a deficiency of the monodeiodinating enzyme.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Biochemistry, Cellular and Molecular Biology, and Physiological Roles of the Iodothyronine Selenodeiodinases.
A. C. Bianco, D. Salvatore, B. Gereben, M. J. Berry, and P. R. Larsen (2002)
Endocr. Rev. 23, 38-89
   Abstract »    Full Text »    PDF »
The Role of the Active Site Cysteine in Catalysis by Type 1 Iodothyronine Deiodinase.
B. C. Sun, J. W. Harney, M. J. Berry, and P. R. Larsen (1997)
Endocrinology 138, 5452-5458
   Abstract »    Full Text »    PDF »


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