Thyroid peroxidase: kinetics, pH optima and substrate dependency.

P R Kootstra; R Wever; J J de Vijlder

doi:10.1530/acta.0.1290328

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Thyroid peroxidase: kinetics, pH optima and substrate dependency.

P R Kootstra·R Wever·J J de Vijlder

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Abstract

The oxidation of iodide, guaiacol and 2,2'-azino-di[3-ethyl-benzthiazoline-(6)-sulphonic acid] and the iodination of tyrosyl residues in bovine serum albumin, catalysed by partly purified thyroid peroxidase, were studied. The enzyme showed pH optima with all electron donors. With the exception of guaiacol, the position of the pH optima depended upon both the electron donor and hydrogen peroxide concentrations. With increased hydrogen peroxide concentrations the optima shifted to lower pH, and with increased iodide concentration to higher pH. For monoiodotyrosine (MIT) formation in bovine serum albumin the position of the pH optimum was also dependent on the hydrogen peroxide concentrations. The position of the pH optimum of the oxidation of guaiacol was pH 9 and independent of substrate and hydrogen peroxide concentrations. It is obvious from these findings that iodination reactions must be studied under well-defined conditions.

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Animals Benzothiazoles Cattle Diiodotyrosine Guaiacol Hydrogen Peroxide Hydrogen-Ion Concentration Iodides Kinetics Monoiodotyrosine Oxidation-Reduction Peroxidase Serum Albumin Substrate Specificity Sulfonic Acids Thyroid Gland Journal Article Research Support, Non-U.S. Gov't

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P R Kootstra, R Wever, J J de Vijlder. 1993. Thyroid peroxidase: kinetics, pH optima and substrate dependency.. https://doi.org/10.1530/acta.0.1290328

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