The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Iodothyronine 5'-deiodinase is present in mouse sublingual gland.

Homogenates from male ddy mouse sublingual glands were incubated with 100 nM [125I]rT3 in the presence of 2 mM dithiothreitol (DTT). Metabolites were analyzed by HPLC or Dowex-50 minicolumn assay. 3,3'-Diiodothyronine and I- were the only appreciable products. Iodide release from rT3 was compatible with the enzymatic nature. The Km and maximum velocity from three separate determinations were 326, 356, and 629 nM and 29.8, 42.1, and 31.3 pmol I- release/mg protein.min, respectively. The deiodinase activity was DTT dependent and had higher affinity for rT3 than for T4 or T3. 6-Propyl-2-thiouracil inhibited the deiodination, which was competitively overcome by DTT. Sublingual 5'-deiodinase activity was approximately 80% of that in the liver, while the submandibular gland showed no deiodination. Our results show the presence of 5'-deiodinase (type I) in mouse sublingual gland for the first time. Selective localization and abundance of the enzyme suggest a previously unrecognized role of the sublingual gland in thyroid hormone physiology.[1]


  1. Iodothyronine 5'-deiodinase is present in mouse sublingual gland. Tanaka, K., Imura, H. Endocrinology (1993) [Pubmed]
WikiGenes - Universities