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• W1567197204 abstract "Abstract The time course of formation of the thyroid iodoprotein 19 S and its subunits (6 S, 7 S, and 12 S) has been studied after intravenous administration of [3H]leucine to normal rats and guinea pigs and after in vitro incorporation in thyroid hemilobes. The uptake of the [3H]leucine by the rat gland in vivo paralleled the disappearance of the radioactivity from the plasma (30 min): the amino acid was rapidly bound to a particulate fraction and was more slowly incorporated into proteins having solubility properties similar to that of thyroglobulin. Sucrose gradient analysis of the newly formed thyroglobulin-like labeled proteins showed the presence of a significant proportion of thyroglobulin and of its half-sized, 12 S subunit even at the earliest labeling interval (10 min). These data suggest that the assembly of the polypeptide chains of thyroglobulin occurs before the newly formed molecules are released from the intracellular membranes. The 6 S and 7 S labeled intermediates appear to be related to newly formed, unstable thyroglobulin molecules, the equilibrium between these units and the fully assembled molecules being shifted toward the latter with increasing labeling times. A similar pattern was observed after pulse labeling guinea pigs in vivo. In this species, however, there is a larger proportion of 12 S subunits derived from dissociation of newly formed and consequently poorly iodinated thyroglobulin molecules. Both in rats and guinea pigs, the sedimentation rate of newly formed thyroglobulin increased progressively from 14 to 19 S with the labeling time. After labeling thyroid hemilobes in vitro, the disappearance of the labeled intermediates 6 S, 7 S, and 12 S was both delayed and incomplete. It appears that the time-dependent disappearance of the labeled subunits 6 S, 7 S, 12 S, and of the unfolded 14 to 17 S species (prethyroglobulin) is related to later chemical modifications which increase the stability of the newly formed thyroglobulin molecules toward dissociation and unfolding. These later modifications include iodination and its oxidative side effects (oxidation of —SH to —S—S—) and addition of the carbohydrate moiety." @default.
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• W1567197204 date "1972-08-01" @default.
• W1567197204 modified "2023-09-26" @default.
• W1567197204 title "Biosynthesis of Thyroid Iodoproteins in Vivo and in Tissue Slices" @default.
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• W1567197204 doi "https://doi.org/10.1016/s0021-9258(19)44997-1" @default.
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