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Colorimetric Assessment of Deiodinase 1 Activity in Human Liver Microsomes Using the Sandell-Kolthoff Reaction
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Iodothyronine deiodinase

D L St Germain1

  • 1Donald L. St. Germain is at the Departments of Medicine and Physiology, Dartmouth Medical School, Lebanon, NH 03756, USA.

Trends in Endocrinology and Metabolism: TEM
|January 1, 1994
PubMed

The iodothyronine deiodinases constitute a family of enzymes that catalyze the removal of iodine atoms from various thyroid hormones (THs) in the thyroid gland and extrathyroidal tissues. As such, they are responsible for both the activation and inactivation of these compounds, and are thus important regulators of TH action. Recently, new insights have been gained into the biochemical characteristics of these proteins and their physiologic roles in TH metabolism. In particular, the availability of affinity-labeling techniques, molecular probes, and specific antisera for these enzymes, and the recent identification of the type I deiodinase as a selenoprotein, have ushered in a new era in the study of thyroid hormone deiodination.

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