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pubmed-article:7371974pubmed:abstractTextPrevious electron-microscopical studies from this laboratory have shown that the thyroglobulin molecule can occur in two different conformations, one ovoid and the other cylindrical. Ovoid molecules are characteristic of well-iodinated thyroglobulin whereas cylindrical molecules are found after low-iodine diet or blocking of iodination. The present study was performed in order to elucidate the possible relation between the molecule conformation and the peroxidase-catalyzed reactions that occur in the thyroid in connection with hormone synthesis. Cylindrical thyroglobulin molecules (from PTU-exposed thyroids) were incubated in different media and the proportion of cylindrical and ovoid molecules after incubation was estimated in electron micrographs. It was found that incubation with glucose-glucose oxidase caused an extensive conversion of cylindrical molecules into ovoid molecules. Peroxidase and/or iodide were not necessary for this change of conformation. It is suggested that this in vitro molecule transformation was the result of an oxidation reaction.lld:pubmed
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pubmed-article:7371974pubmed:articleTitleConformational change of the thyroglobulin molecule induced by oxidation in vitro.lld:pubmed
pubmed-article:7371974pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:7371974pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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