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PubMed1976

A comparison of thyrotropin- and dibutyryl cyclic AMP- induced thyroglobulin iodination in cultured human thyroid cells.

The relative degree of 125-I labelling of thyroglobulin-- bound mono-iodotyrosine (MIT) and di-iodotyrosine (DIT) in isolated, cultured human thyroid cells has been compared following exposure of 125-I supplemented cells to 100 mU/ml of bovine thyrotropin (TSH) or 1.0 mM dibutyryl cyclic AMP (dBcAMP) for 96 hours. Pronase digestion of the lysed cells and Sephadex G-10 fractionation of the digested lysates revealed a predominance of [125-I]MIT over [125-I]DIT in both sets of experimental cells as well as in controls. Levels of [125-I]DIT, however, were only enhanced above control values in cells incubated with TSH. These findings suggest that an increase in availability of intracellular iodide, following cellular exposure to TSH, may facilitate a preferential synthesis of DIT relative to that of MIT. This theory offers an explanation for the differential effects of TSH and dibutyryl cyclic AMP on the levels of newly--synthesised T4 recovered from the cells used in this study, and from the culture medium in a previous investigation.

Bucladesine↗
PubMed1985

Detection of a catalytic intermediate of peroxidase in hog thyroid microsomes.

A catalytic intermediate, Compound II of peroxidase was detected spectrophotometrically in thyroid microsomes. From comparison with the spectral data on purified thyroid peroxidase, the content of the peroxidase was estimated to be 0.019 nmol per mg of the microsomal protein, being about one-eighth of the amount of cytochrome b5. It was concluded that thyroid peroxidase exhibits the same peroxidase activity for guaiacol or ascorbate in the free and the microsome-bound forms.

Animals↗