The Isolation and Purification of Thyroid Peroxidase

摘要: Abstract A procedure for the extraction and isolation of peroxidase in pig thyroid glands has been described. The enzyme purified by gel filtration diethylaminoethyl chromatography, its spectral properties suggest that is a typical hemoprotein peroxidase, while experiments have shown it to molecular weight 104,000. specific activity preparation was significantly higher than other reported preparations. can oxidize 48.9 µmoles guaiacol per min mg protein, or 7.35 iodide ion protein. rate constant, k1, between hydrogen peroxide found be 1.1 x 107 m-1 sec-1 at pH 7.4. kd, Complex II donor had value 105 7.4, 1.3 KI 7.0. temperature optimum 37–40°. iodinate tyrosine thyroglobulin.