1984
DOI: 10.1210/endo-115-1-33
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Abstract: Two proteases were purified from lysosomal supernatants of hog thyroids. The first step of the purification by diethylaminoethyl cellulose chromatography separated the two proteases, which were shown to have quite similar properties with respect to 2-mercaptoethanol requirement and pH optima for benzoyl-L-arginine-2-naphthylamide (BANA) hydrolytic activity, and inhibition by sulfhydryl inhibitors. One of the proteases, designated as thiol protease-1 (TP-1), was further purified by gel filtration (Sephacryl S-2… Show more

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Cited by 13 publications
(1 citation statement)
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“…Several different thiol proteases have been de¬ scribed in thyroid tissue (Dunn & Dunn 1982b;Nakagawa & Ohtaki 1984, and further studies are required to determine their specific roles in Tg proteolysis. Of particular interest in this connection is a recent report by Nakagawa 8c Ohtaki (1985) describing a thiol protease that releases T4 very efficiently from a naturally occur¬ ring 19 amino acid T4-containing fragment of Tg originally described by Rawitch et al (1983), but which displays only little activity in liberating T4 from intact Tg.…”
Section: Discussionmentioning
confidence: 99%
“…Several different thiol proteases have been de¬ scribed in thyroid tissue (Dunn & Dunn 1982b;Nakagawa & Ohtaki 1984, and further studies are required to determine their specific roles in Tg proteolysis. Of particular interest in this connection is a recent report by Nakagawa 8c Ohtaki (1985) describing a thiol protease that releases T4 very efficiently from a naturally occur¬ ring 19 amino acid T4-containing fragment of Tg originally described by Rawitch et al (1983), but which displays only little activity in liberating T4 from intact Tg.…”
Section: Discussionmentioning
confidence: 99%