甲状腺Peroxidase活性に及ぼす甲状腺刺戟ホルモンの影響
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概要
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An attempt was made by the author to devise a new method of determining the active peroxidase of thyroid gland by modified Randall's method of determining active peroxidase, by adding K.I. & 1-tyrosine to a substrate and by evaluating the rate of H<SUB>2</SUB>O<SUB>2</SUB> loss with use of Warburg's manometer and through which variation of the amino iodides could be traced.<BR>By means of the manometric method, the influence of TSH on peroxidase was examined by adding TSH to the substrate and paperchromatographically tested of the reacted solution.<BR>The following results were obtained upon analysis of the formed substances : <BR>1. TSH directly accelerates activation of peroxidase.<BR>2. No specific character could be observed whether peroxidases are from vegetative or animal sources on the oxidation process of the iodides based on the fact that they are equally activated in the presence of TSH 10<SUP>-2</SUP>-10<SUP>-3</SUP>-10<SUP>-4</SUP> J.S.U., whether standard product of peroxidase employed, or tried with the thyroid homogenate of guinea pigs.<BR>3. Direct relationship has been shown between the concentrated TSH and the rate of increased activity in TSH concentration range of 10<SUP>-2</SUP>-10<SUP>-3</SUP>-10<SUP>-4</SUP> J.S.U.<BR>4. Paperchromatographic examination of solution with the standard peroxidase revealed the fact that formotion of monoiodotyrosine and diiodotyrosine at TSH 10<SUP>-2</SUP> J.S.U. was most increased, and the rate of amino iodide decrease was noted in the order of TSH 10<SUP>-2</SUP>-10<SUP>-3</SUP>-10<SUP>-4</SUP>J.S.U. The formation of both monoiodotyrosine and diiodotyrosine was observed with the thyroid homogenate of male guinea pigs also.<BR>5. It is assumed that increased formation of amino iodides was due to activation of peroxidase by TSH which in turn seems to accelerate oxidation of iodide and the other iodizing processes.
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