| Budget Amount *help |
¥4,400,000 (Direct Cost: ¥4,400,000)
Fiscal Year 1986: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1985: ¥3,600,000 (Direct Cost: ¥3,600,000)
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| Research Abstract |
A modified purification method of human thyroid peroxidase from thyroids of patients with Graves' disease was established using an immunoaffinity chromatography with a monoclonal antibody. This is so far the best in specificity, yield, and speed to prepare it's native form. The enzyme is almost identical to the nature of porcine enzyme in spectra, activity and other properties. In the experiments with porcine enzyme, thyroid peroxidase was found to cause the two-electrons oxidation of glutathione through phenoxyl cation of tyrosine in the presence of <H_2> <O_2> . In the experiment with regulation of thyroid cell functions, porcine thyroid microsomes were found to actively transport calcium ion, suggesting that, through this active transport mechanism, this ion serves as an important factor to regulate intracellular transmittance of thyroid cell functions. Further, it was observed that a unique electron transport system regulated by calcium and ATP exists in thyroid plasma membrane serving as an oxidase system for iodination of thyroglobulin (hormone biosynthesis).
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