Peroxidase Activity in Thyroid Gland and Partial Purification of the Enzyme

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Abstract
Peroxidase activity (substrates: guaiacol, iodide or leucodyes) is detected in intestine, thyroid gland, stomach, and liver. A thyroid peroxidase preparation from a sub-cellular fraction shows peroxidase and I131-incorporating activities which are equally inhibited by cyanide, azkie, 3-amino-12,4-triazole or thiouracil, while p-aminobenzoate and rhodanate suppress the iodinating action more strongly than peroxidase activity. The preparation possesses peroxidase purified about 20 fold, which gives 1 inactive protein and 2 active peroxidases in paper electrophoresis at pH 7.0. A possible participation of peroxidase in thyroidal hormone biosynthesis is discussed.