Purification and characterization of a cytosolic protein enhancing GSH-dependent microsomal iodothyronine 5'-monodeiodination.
A protein has been purified from rat liver cytosol which promoted GSH-responsive iodothyronine 5'-deiodinase activities in rat kidney microsomes. The factor behaved as a basic protein with an Mr of 11,000. It was active as a GSH-disulfide transhydrogenase with beta-hydroxyethyl disulfide as an acceptor and was also active in stimulating calf thymus ribonucleotide reductase with one-third the potency of native calf thymus glutaredoxin. Another basic protein, which degraded iodothyronines oxidatively, was also identified in the cytosolic preparations; this co-purified with soluble protein factor in the earlier purification stages and was partially separated from this factor by CM-cellulose chromatography. The glutaredoxin-like protein present in rat liver and kidney cytosol could provide a physiologic regulatory mechanism for GSH-dependent 5'-monodeiodination of iodothyronines.
D000818:Animals; D003600:Cytosol / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D054477:Glutaredoxins; D005978:Glutathione / Q000494:pharmacology*; D007453:Iodide Peroxidase / Q000378:metabolism*; D007668:Kidney / Q000378:metabolism; D008297:Male; D008861:Microsomes / Q000378:metabolism; D010088:Oxidoreductases; D010544:Peroxidases / Q000378:metabolism*; D011490:Protein Disulfide Reductase (Glutathione) / Q000378:metabolism; D011506:Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D051381:Rats; D013880:Thioredoxin-Disulfide Reductase / Q000494:pharmacology; D013879:Thioredoxins / Q000494:pharmacology
D054477:Glutaredoxins; D011506:Proteins; D013879:Thioredoxins; D010088:Oxidoreductases; D010544:Peroxidases; D007453:Iodide Peroxidase; D013880:Thioredoxin-Disulfide Reductase; D011490:Protein Disulfide Reductase (Glutathione); D005978:Glutathione