Abstract
The iodoamino acid composition of hog thyroglobulin was determined by an improved ion-exchange chromatographic method over a wide range of thyroglobulin iodine content (0.16–1.10%), using mostly chromatographically fractionated preparations which had a narrower distribution of iodine content and were free of heavier or lighter components. It has been found that the iodoamino acid distribution is strictly related to the degree of iodination of the protein, except for one minor, presumably anomalous, subfraction in which a slight deviation was observed. The characteristic variation of the content of each iodoamino acid, i.e. monoiodotyrosine, diiodotyrosine, triiodothyronine or thyroxine, with increasing levels of iodination has revealed the special feature of hormonogenesis occurring within the molecule of thyroglobulin. The iodoamino acid composition of the 12-S subunit formed by succinylation of thyroglobulin was found to differ significantly from that of the fraction resistant to dissociation. All these data strongly supported the concept that the structure of thyroglobulin plays an essential role in the biosynthesis of iodoamino acids.
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