Characterization of type-II thyroxine 5'-deiodinase activity in rat Harderian gland.
Thyroxine 5'-deiodinase activity was studied in male rat Harderian gland homogenates. The reaction rate was proportional to the tissue content in the homogenate and dependent on pH, with an optimum pH of 7.0, and temperature, between 4-37 degrees C. 5'-deiodinase activity was increased by dithiothreitol (DTT) in a dose-dependent manner, and inhibited moderately by propylthiouracil (PTU) and strongly by iopanoic acid (IA). Thyroidectomy enhanced the enzymatic activity (30-fold above the control value) but this increase is totally prevented by the in vivo iopanoic acid treatment. Thyroxine 5'-deiodinase activity was also dependent on T4 concentration (Km = 3.3 nM; Vmax = 10 fmol 125I-released/mg protein/h) and exhibited a nyctohemeral rhythmicity with a maximal activity at 03.00 h (4-fold above basal values) and minimal activity between 12.00-21.00 h.
D000818:Animals; D002940:Circadian Rhythm; D004229:Dithiothreitol / Q000494:pharmacology; D006243:Harderian Gland / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007453:Iodide Peroxidase / Q000378:metabolism*; D007480:Iopanoic Acid / Q000494:pharmacology; D007765:Lacrimal Apparatus / Q000201:enzymology*; D051381:Rats; D013965:Thyroidectomy
D007453:Iodide Peroxidase; D007480:Iopanoic Acid; D004229:Dithiothreitol